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Isoenzymes

  • Chapter
Alkaline Phosphatase

Abstract

The identity of enzymes cannot be determined exactly as long as one enzyme is mixed with others of the same group.1

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References

  1. Davis, D. R., The phosphatase activity of spleen extracts, Biochem. J., 28, 529, 1934.

    Google Scholar 

  2. Hommerberg, C., Zur Kenntnis der Spezifizität tierischer Phosphatase, Z. Physiol. Chem., 185, 123, 1929.

    CAS  Google Scholar 

  3. Bodansky, O., Are the phophatases of bone, kidney, intestine and serum identical? The use of bile acids in their differentiation, J. Biol. Chem., 118, 341, 1937.

    CAS  Google Scholar 

  4. Cloetens, R., Identification de deux phosphatases “alcalines” dans les organes animaux, Enzymologia, 6, 46, 1939.

    CAS  Google Scholar 

  5. Moog, F., The physiological significance of the phosphomonoesterase, Biol. Rev., 21, 41, 1946.

    CAS  Google Scholar 

  6. King, E. J., Acid and alkaline phosphatase, in: Lectures on the Scientific Basis of Medicine, Vol. 3, pp. 187–218, British Postgraduate Medical Federation, Athlone Press, London, 1953–1954.

    Google Scholar 

  7. Gutman, A. B., Serum alkaline phosphatase activity in diseases of the skeletal and hepatobiliary systems, Am. J. Med., 27, 875, 1959.

    CAS  Google Scholar 

  8. Gomori, G., Pitfalls in histochemistry, Ann. N. Y. Acad. Sci., 50, 968, 1950.

    CAS  Google Scholar 

  9. Roche, J., and Sarles, H., Spécificité d’organe des phosphatases alcalines animales et origine de la phosphatase alcaline du sérum humain au cours des hyperphosphatasémies, Biochim. Biophys. Acta, 5, 275, 1950.

    CAS  Google Scholar 

  10. Markert, C. L., and Moller, F., Multiple forms of enzymes; tissue, ontogenetic and species specific patterns, Proc. Natl Acad. Sci. U.S.A., 45, 753, 1951.

    Google Scholar 

  11. Markert, C. L., The molecular basis for isozymes, Ann. N. Y. Acad. Sci., 151, 14, 1968.

    CAS  Google Scholar 

  12. International Union of Pure and Applied Chemistry and International Union of Biochemistry, Enzyme Nomenclature, p. 23, Elsevier, Amsterdam, 1973.

    Google Scholar 

  13. Nagode, L. A., Koestner, A., and Steinmeyer, C. L., Organ-identifying properties of alkaline phosphatases from canine tissues, Clin. Chim. Acta, 26, 45, 1969.

    CAS  Google Scholar 

  14. Schlesinger, M. J., and Andersen, L., Multiple molecular forms of the alkaline phosphatase of Escherichia coli, Ann. N. Y. Acad. Sci., 151, 159, 1968.

    CAS  Google Scholar 

  15. Kelley, P. M., Neumann, P. A., Shriefer, K., Cancedda, F., Schlesinger, M. J., and Bradshaw, R. A., Amino acid sequence of Escherichia coli alkaline phosphatase: Amino and carboxyl terminal sequences and variations between two isozymes, Biochemistry, 12, 3499, 1973.

    CAS  Google Scholar 

  16. Shaw, C. R., Isoenzymes: Classification, frequency and significance, Int. Rev. Cytol., 25, 297, 1969.

    CAS  Google Scholar 

  17. Wilkinson, J. H., Isoenzymes, 2nd ed., p. 1, J. B. Lippincott, Philadelphia, 1970.

    Google Scholar 

  18. Byers, D. A., Fernley, H. N., and Walker, P. G., Studies on alkaline phosphatases: Catalytic activity of human-placental alkaline-phosphatase variants, Eur. J. Biochem., 29, 205, 1972.

    CAS  Google Scholar 

  19. Fishman, W. H., and Ghosh, N. K., Isoenzymes of human alkaline phosphatase, Adv. Clin. Chem., 10, 255, 1967.

    CAS  Google Scholar 

  20. Neumann, H., Wilson, K. J., Hauck-Granoth, R., and Haran-Ghera, N., A comparative biochemical study of alkaline phosphatases in normal and leukemic mice, Cancer Res., 31, 1695, 1971.

    CAS  Google Scholar 

  21. Neumann, H., Substrate selectivity in the action of alkaline and acid phosphatases, J. Biol. Chem., 243, 4671, 1968.

    Google Scholar 

  22. International Union of Pure and Applied Chemistry and International Union of Biochemistry, Nomenclature of multiple forms of enzymes: Recommendations (1976), J. Biol. Chem., 252, 5939, 1977.

    Google Scholar 

  23. Gorman, J. A., and Hu, A. S. L., The separation and partial characterization of L-histidinol phosphatase and an alkaline phosphatase of Saccharomyes cerevisiae, J. Biol. Chem., 244, 1645, 1969.

    CAS  Google Scholar 

  24. Bitar, K., and Reinhold, J. G., Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf and man, Biochim. Biophys. Acta, 268, 422, 1972.

    Google Scholar 

  25. Reis, J. L., The specificity of phosphomonoesterases in human tissue, Biochem, J., 48, 548, 1951.

    CAS  Google Scholar 

  26. Ahmed, Z., and Reis, J. L., The activation and inhibition of 5-nucleotidase, Biochem. J., 69, 386, 1958.

    CAS  Google Scholar 

  27. Tabachnick, J., and Perlish, J. S., Studies on the biochemistry of epidermis. III. Content and some characteristics of 5 nucleotidases, pyrophosphatases and phosphomonoesterases of albino guinea pig and rat epidermis, J. Invest. Dermatol., 48, 587, 1967.

    CAS  Google Scholar 

  28. Douglas, A. P., Kerley, R., and Isselbacher, K. J., Preparation and characterization of the lateral and basal plasma membranes of the rat intestinal epithelial cell, Biochem. J., 128, 1329, 1972.

    CAS  Google Scholar 

  29. Goldberg, D. M., and Belfield, A., Reciprocal relationship of alkaline phosphatase and 5’- nucleotidase in human bone, Nature (London), 247, 286, 1974.

    CAS  Google Scholar 

  30. Schwartz, M. K., and Bodansky, O., Properties of 5-nucleotidase activity in human serum and applications in diagnosis, Amer. J. Gin. Pathol., 42, 572, 1964.

    CAS  Google Scholar 

  31. Schwartz, M. K., and Bodansky, O., Serum 5-nucleotidase in patients with cancer, Cancer, 18, 886, 1965.

    CAS  Google Scholar 

  32. Melnkovych, G., Swayze, M. A., Bishop, C., and Costlow, C., Effect of prednisolone on esterases in heteroploid cells of human origin, Biochim. Biophys. Acta, 184, 672, 1969.

    Google Scholar 

  33. Hill, P. G., and Sammons, H. G., An assessment of 5’-nucleotidase as a liver function test, Q. J. Med., 36, 451, 1967.

    Google Scholar 

  34. Kowlessar, O. D., Pert, J. H., Haeffner, L. J., and Sleisenger, M. H., Localization of 5’-nucleotidase and non-specific alkaline phosphatase by starch gel electrophoresis, Proc. Soc. Exp. Biol. Med., 100, 191, 1959.

    CAS  Google Scholar 

  35. Moss, D. W., Separation of serum 5’-nucleotidase and nonspecific alkaline phosphatase activities, Nature (London), 209, 806, 1966.

    CAS  Google Scholar 

  36. Folley, S. J., and Kay, H. D., The phosphatases, Ergebn. Enzymforsch., 5, 159, 1936.

    CAS  Google Scholar 

  37. Norman, A. W., Mircheff, A. K., Adams, T. H., and Spielvogel, A., Studies on the mechanism of action of calciferol. III. Vitamin D mediated increase of intestinal brush border alkaline phosphatase activity, Biochim. Biophys. Acta, 215, 358, 1970.

    Google Scholar 

  38. Melnykovych, G., and Costlow, C. C., Release of surface-associated phosphoesterases from HeLa cells by ficin, Proc. Soc. Exp. Bio. Med., 138, 1101, 1971.

    CAS  Google Scholar 

  39. Robbins, J. H., Electrophoresis of mammalian aldehyde deyhydrogenase, Arch. Biochem. Biophys., 114, 585, 1966.

    CAS  Google Scholar 

  40. Ressler, N., Interpretation of subbands of lactic dehydrogenase isoenzymes, Nature (London), 215, 284, 1967.

    CAS  Google Scholar 

  41. Eguchi, M., Sawaki, M., and Suzuki, Y., Multiple forms of midgut alkaline phosphatase in the silkworm: Separation and comparison of two isoenzymes, Insect Biochem., 2, 167, 1972.

    CAS  Google Scholar 

  42. Beratis, N. G., Seegers, W., and Hirschhorn, K., Properties of placental alkaline phosphatase. I. Molecular size and electrical charge of the various electrophoretic components of the six common phenotypes, Biochem. Genet., 4, 689, 1970.

    CAS  Google Scholar 

  43. Hosoyama, Y., Fukuda, Y., and Shimadate, T., Paper chromatography of alkaline phosphatase isoenzymes, Clin. Chim. Acta, 18, 141, 1967.

    CAS  Google Scholar 

  44. Schlesinger, M. J., Reynolds, J. A., and Schlesinger, S., Formation and localization of the alkaline phosphatase of Escherichia coli, Ann. N. Y. Acad. Sci., 166, 368, 1969.

    CAS  Google Scholar 

  45. Ostrowski, W., and Barnard, E. E., Acid phosphomonoesterase of human prostate: Phosphate transfer reactions and comparison with alkaline phosphatase, Biochim. Biophys. Acta, 250, 131, 1971.

    CAS  Google Scholar 

  46. Peacock, A. C., Reed, R. A., and Highsmith, E. M., Ethanol fractionation of human serum alkaline phosphatase, Clin. Chim. Acta, 8, 914, 1963.

    CAS  Google Scholar 

  47. Engström, L., Studies on bovine liver alkaline phosphatase, purification, phosphate incorporation, Biochim. Biophys. Acta, 92, 71, 1964.

    Google Scholar 

  48. Kuan, S. S., Martin, W. G., and Patrick, H., Alkaline phosphatase in the chick: Partial characterization of the tissue isozymes, Proc. Soc. Exp. Biol. Med., 122, 172, 1966.

    CAS  Google Scholar 

  49. Schneiderman, H., Alkaline phosphatase relationships in Drosophila, Nature (London), 216, 604, 1967.

    CAS  Google Scholar 

  50. Dorn, G. L., Purification of two alkaline phosphatases from Aspergillus nidulans, Biochim. Biophys. Acta, 132, 190, 1967.

    CAS  Google Scholar 

  51. Mills, G. T., and Smith, E. E. B., The electrophoresis of enzymes on filter paper, Biochem. J., 49, 6, 1951.

    Google Scholar 

  52. Delcourt, A., and Delcourt, R., Séparation et localisation des enzymes dans les liquides organiques par électrophorèse sur papier, C. R. Soc. Biol., 147, 1104, 1953.

    CAS  Google Scholar 

  53. Baker, R. W. R., and Pellegrino, C., Separation and detection of serum enzymes by paper electrophoresis, Scand. J. Clin. Lab. Invest., 6, 94, 1954.

    CAS  Google Scholar 

  54. Taleisnik, S., Paglini, S., and Zeitune, V., Localisation de la phosphatase alcaline du serum das les fractions protéiniques séparées par électrophorèse, C. R. Soc. Biol., 149, 1790, 1955.

    Google Scholar 

  55. Wolfson, W. Q., Location of alpha-2 globulin by demonstration of alkaline phosphatase during paper electrophoresis, Nature (London), 180, 550, 1957.

    CAS  Google Scholar 

  56. Eisfeld, G., and Koch, E., Das Verhalten der alkalischen und sauren Serumphosphatase des Menschen bei der Papierelektrophorese, Z. Gesamte Inn. Med., 9, 514, 1954.

    CAS  Google Scholar 

  57. Keiding, N. R., Differentiation into three fractions of serum alkaline phosphatase and the behaviour of the fractions in diseases of bone and liver, Scand. J. Clin. Lab. Invest., 11, 106, 1959.

    CAS  Google Scholar 

  58. Estborn, B., Visualisation of acid and alkaline phosphatase after starch gel electrophoresis of seminal plasma, serum and bile, Nature (London), 184, 1636, 1959.

    CAS  Google Scholar 

  59. Rosenberg, I. N., Zone electrophoretic studies of serum alkaline phosphatase, J. Clin. Invest., 38, 630, 1959.

    CAS  Google Scholar 

  60. Kowlessar, O. D., Haeffner, L. J., and Riley, E. M., Localization of serum leucine aminopeptidase, 5-nucleotidase and nonspecific alkaline phosphatase by starch-gel electrophoresis: Clinical and biochemical significance in disease states, Ann. N. Y. Acad. Sci., 94, 836, 1961.

    CAS  Google Scholar 

  61. Chiandussi, L., Greene, S. F., and Sherlock, S., Serum alkaline phosphatase fractions in hepatobiliary and bone diseases, Clin. Sci., 22, 425, 1962.

    CAS  Google Scholar 

  62. Hodson, A. W., Latner, A. L., and Raine, L., Iso-enzymes of alkaline phosphatase, Clin. Chim. Acta, 7, 255, 1962.

    CAS  Google Scholar 

  63. Taswell, H. F., and Jeffers, D. M., Isoenzymes of serum alkaline phosphatase in hepatobiliary and skeletal disease, Amer. J. Clin. Pathol., 40, 349, 1963.

    CAS  Google Scholar 

  64. Meade, B. W., and Rosalki, S. B., Serum enzyme activity in normal pregnancy and the newborn, J. Obstet. Gynaecol. Br. Commonw., 70, 693, 1963.

    CAS  Google Scholar 

  65. Aalund, O., Rendel, J., and Freedland, R. A., Isolation and characterisation of ovine serum alkaline phosphatases, Biochim. Biophys. Acta, 110, 113, 1965.

    CAS  Google Scholar 

  66. Bach, M. L., Signer, E. R., Levinthal, C., and Sizer, I. W., The electrophoretic patterns of alkaline phosphatase from various E. coli mutants, Fed. Proc. Fed. Am. Soc. Exp. Biol., 20, 255, 1961.

    Google Scholar 

  67. Boyer, S. H., Alkaline phosphatase in human sera and placentae, Science, 134, 1002, 1961.

    CAS  Google Scholar 

  68. Boyer, S. H., Human organ alkaline phosphatases: Discrimination by several means including starch-gel electrophoresis of antienzyme-enzyme supernatant fluids, Ann. N. Y. Acad. Sci., 103, 938, 1963.

    CAS  Google Scholar 

  69. Moss, D. W., and King, E. J., Properties of alkaline phosphatase fractions separated by starch gel electrophoresis, Biochem. J., 84, 192, 1962.

    CAS  Google Scholar 

  70. Robson, E. B., and Harris, H., Further studies on the genetics of placental alkaline phosphatase, Ann. Hum. Genet. London, 30, 219, 1967.

    CAS  Google Scholar 

  71. Schlesinger, M. J., and Olsen, R., Expression and localization of Escherichia coli alkaline phosphatase synthesized in Salmonella typhimurium cytoplasm, J. Bacteriol., 96, 1601, 1968.

    CAS  Google Scholar 

  72. Cox, R. P., and Griffin, M. J., Alkaline phosphatase. 1. Comparison of the physical and chemical properties of enzyme preparations from mammalian cell cultures, various animal tissues and Escherichia coli, Arch. Biochem. Biophys., 122, 552, 1967.

    CAS  Google Scholar 

  73. Warnock, M. L., Characterisation of tissue and serum alkaline phosphatase, Clin. Chim. Acta, 14, 156, 1966.

    CAS  Google Scholar 

  74. Beckman, L., and Beckman, G., A genetic variant of placental alkaline phosphatase with unusual electrophoretic properties, Acta Genet. (Basel), 18, 543, 1968.

    CAS  Google Scholar 

  75. Ornstein, L., Disc electrophoresis. I. Background and theory, Ann. N. Y. Acad. Sci., 121, 321, 1964.

    Google Scholar 

  76. Davis, B. J., Disc electrophoresis. II. Method and application to human serum proteins, Ann. N. Y. Acad. Sci., 121, 404, 1964.

    Google Scholar 

  77. Smith, I., Lightstone, P. J., and Perry, J. D., Separation of human tissue alkaline phosphatases by electrophoresis on acrylamide disc gels, Clin. Chim. Acta, 19, 499, 1968.

    CAS  Google Scholar 

  78. Kaplan, M. M., and Rogers, L., Separation of human serum-alkaline-phosphatase isoenzymes by poly acrylamide gel electrophoresis, Lancet, 2, 1029, 1969.

    CAS  Google Scholar 

  79. Canapa-Anson, R., and Rowe, D. J. F., Electrophoretic separation of tissue specific alkaline phosphatases, J. Clin. Pathol., 23, 499, 1970.

    CAS  Google Scholar 

  80. Johnson, R. B., Ellingboe, K., and Gibbs, P., A study of various electrophoretic and inhibition techniques for separating serum alkaline phosphatase isoenzymes, Clin. Chem., 18, 110, 1972.

    CAS  Google Scholar 

  81. Freeman, S. B., A comparison of certain isozyme patterns in lobeless and normal embroys of the snail, Ilyanassa obsoleta, J. Embryol. Exp. Morphol., 26, 339, 1971.

    CAS  Google Scholar 

  82. Korner, N. H., Distribution of alkaline phosphatase in serum protein fractions, J. Clin. Pathol, 15, 195, 1962.

    CAS  Google Scholar 

  83. Posen, S., Neale, F. C., Birkett, D. J., and Brudenell-Woods, J., Intestinal alkaline phosphatase in human serum, Am. J. Gin. Pathol., 48, 81, 1967.

    CAS  Google Scholar 

  84. Fritsche, H. A., and Adams-Park, H. R., Cellulose acetate electrophoresis of human serum and tissue alkaline phosphatase isoenzymes, Clin. Chem., 18, 417, 1972.

    CAS  Google Scholar 

  85. Bergerman, J., and Blethen, S., Determination of alkaline phosphatase isoenzymes, Clin. Chim. Acta, 36, 389, 1972.

    CAS  Google Scholar 

  86. Rhone, D. P., and Mizuno, F. M., Profiles of alkaline phosphatase isoenzymes in serum using cellulose acetate electrophoresis and organ-specific inhibitors, Am. J. Clin. Pathol., 59, 531, 1973.

    CAS  Google Scholar 

  87. Latner, A. L., Parsons, M., and Skillen, A. W., Isoelectric focusing of alkaline phosphatases from human kidney and calf intestine, Enzymologia, 40, 1, 1971.

    CAS  Google Scholar 

  88. Smith, I., Lightstone, P. J., and Perry, J. D., Isoelectric focusing of alkaline phosphatases: A focusing-disc electrophoresis transfer technique, Clin. Chim. Acta, 35, 59, 1971.

    CAS  Google Scholar 

  89. Csopak, H., Jonsson, M., and Hallberg, B., Isoelectric fractionation of the Escherichia coli alkaline phosphatase and resolution of the purified enzyme into isoenzymes, Acta Chem. Scand., 26, 2412, 1972.

    CAS  Google Scholar 

  90. Nordentoft-Jensen, B., Differentiation between the electrophoretic pattern of serum alkaline phosphatase in bone disease and liver disease, Clin. Sci., 26, 299, 1964.

    CAS  Google Scholar 

  91. Haije, W. G., and De Jong, M., Iso-enzyme patterns of serum alkaline phosphatase in agar-gel electrophoresis, and their clinical significance, Clin. Chim. Acta, 8, 620, 1963.

    CAS  Google Scholar 

  92. Yong, J. M., Origins of serum alkaline phosphatase, J. Gin. Pathol., 20, 647, 1967.

    CAS  Google Scholar 

  93. Nerenberg, S. T., and Pogojeff, G., Laboratory diagnosis of specific organ diseases by means of combined serum isoenzyme patterns, Am. J. Gin. Pathol., 51, 429, 1969.

    CAS  Google Scholar 

  94. Rawstron, J. R., and Ng, S. H., Rapid electrophoresis of alkaline phosphatase isoenzymes, Clin. Chim. Acta, 32, 303, 1971.

    CAS  Google Scholar 

  95. Dymling, J. F., Separation of serum and placental alkaline phosphatase by agarose gel electrophoresis and Sephadex chromatography, Scand. J. Gin. Lab. Invest., 18, 129, 1966.

    CAS  Google Scholar 

  96. Demetriou, J. A., and Beattie, J. M., Electrophoretic separation on agarose thin film of isoenzymes of alkaline phosphatase from human serum and tissue, Clin. Chem., 17, 290, 1971.

    CAS  Google Scholar 

  97. Ewen, L. M., Separation of alkaline phosphatase isoenzymes and evaluation of the clinical usefulness of this determination, Am. J. Clin. Pathol., 61, 142, 1974.

    CAS  Google Scholar 

  98. Peacock, A. C., and Garner, V., Separation of serum alkaline phosphatase in normal subjects by continuous-flow electrophoresis, Clin. Chim. Acta, 8, 314, 1963.

    CAS  Google Scholar 

  99. Ghosh, N. K., and Fishman, W. H., Purification and properties of molecular-weight variants of human placental alkaline phosphatase, Biochem. J., 779, 1968.

    Google Scholar 

  100. Butterworth, P. J., Moss, D. W., Pitkanen, E., and Pringle, A., Some characteristics of alkaline phosphatase in human urine, Clin. Chim. Acta, 11, 220, 1965.

    CAS  Google Scholar 

  101. Evered, D. F., and Steenson, T. I., Citrate inhibition of alkaline phosphatase, Nature (London), 202, 491, 1964.

    CAS  Google Scholar 

  102. Zittle, C. A., and Della Monica, E. S., Effects of borate and other ions on the alkaline phosphatase of bovine milk and intestinal mucosa, Arch. Biochem., 26, 112, 1950.

    CAS  Google Scholar 

  103. Kitchener, P. N., Neale, F. C., Posen, S., and Brudenell-Woods, J. B., Alkaline phosphatase in maternal and fetal sera at term and during the puerperium, Am. J. Gin. Pathol., 44, 654, 1965.

    CAS  Google Scholar 

  104. Posen, S., Cornish, C. J., Home, M., and Saini, P. K., Placental alkaline phosphatase and pregnancy, Ann. N. Y. Acad. Sci., 166, 733, 1969.

    CAS  Google Scholar 

  105. Thomas, D. M., and Harris, H., Comparison of thermo-stabilities of different human placental alkaline phosphatase phenotypes, Ann. Hum. Genet. (London), 35, 221, 1971.

    CAS  Google Scholar 

  106. Beratis, N. G., and Hirschhorn, K., Properties of placental alkaline phosphatase. III. Thermostability and urea inhibition of isolated components of the three common phenotypes, Biochem. Genet., 6, 1, 1972.

    CAS  Google Scholar 

  107. Warnock, M. L., Intestinal phosphatase and fat absorption, Proc. Soc. Exp. Biol. Med., 129, 768, 1968.

    CAS  Google Scholar 

  108. Cornish, C. J., Studies on bone alkaline phosphatase, M.S. thesis, University of Sydney, 1973.

    Google Scholar 

  109. Fishman, L., Inglis, N. R., and Fishman, W. H., Preparation of two antigens of human liver isoenzymes of alkaline phosphatase, Clin. Chim. Acta, 34, 393, 1971.

    CAS  Google Scholar 

  110. Warnes, T. W., Alkaline phosphatase, Gut, 13, 926, 1972.

    CAS  Google Scholar 

  111. Healy, P. J., Quantitative analysis of serum alkaline phosphatase isoenzyme activity, Clin. Chim. Acta, 55, 407, 1974.

    CAS  Google Scholar 

  112. Kaplan, M. M., Alkaline phosphatase, Gastroenterology, 62, 452, 1972.

    CAS  Google Scholar 

  113. Rhone, D. P., Mizuno, F. M., and Gidaspow, H., Profiles of serum isoenzymes of alkaline phosphatase in hepatobiliary disorders using cellulose acetate electrophoresis and organ-specific inhibitors, Ann. Clin. Lab. Sci., 3, 353, 1973.

    CAS  Google Scholar 

  114. Du Buisson, J., and Pepler, W. J., The diagnostic patterns of the iso-enzymes of serum non- specific alkaline phosphatase, S. Afr. Med. J., 40, 696, 1966.

    Google Scholar 

  115. Posen, S., Kleerekoper, M., and Cornish, C., Serum alkaline phosphatase in the diagnosis of metabolic bone disorders, in: Clinical Aspects of Metabolic Bone Disease (Frame, B., Parfitt, A. M., and Duncan, H., eds.), p. 74, Excerpta Medica, Amsterdam, 1973.

    Google Scholar 

  116. Robinson, J. C., and Pierce, J. E., Differential action of neuraminidase on human serum alkaline phosphatase, Nature (London), 204, All, 1964.

    Google Scholar 

  117. Rhone, D. P., White, F. M., and Gidaspow, H., The isoenzymes of alkaline phosphatase in sera of normal pregnancy at term, Obstet. Gynecol., 43, 31, 1974.

    CAS  Google Scholar 

  118. Walker, A. W., and Pollard, A. C., Observations on serum alkaline phosphatase electrophoretic patterns on poly aery lamide gel, Clin. Chim. Acta, 34, 1971.

    Google Scholar 

  119. Newton, M.A., The clinical application of alkaline phosphatase electrophoresis, Q. J. Med., 36, 17, 1967.

    CAS  Google Scholar 

  120. Jennings, R. C., Brocklehurst, D., and Hirst, M., A comparative study of alkaline phosphatase enzymes using starch-gel electrophoresis and Sephadex gel-filtration with special reference to high molecular weight enzymes, Clin. Chim. Acta, 30, 509, 1970.

    CAS  Google Scholar 

  121. Robson, E. B., and Harris, H., Genetics of the alkaline phosphatase polymorphism of the human placenta, Nature (London), 207, 1257, 1965.

    CAS  Google Scholar 

  122. Fahey, J. L., McCoy, P. F., and Goulian, M., Chromatography of serum proteins in normal and pathologic sera: The distribution of protein bound carbohydrate and cholesterol, siderophilin, thyroxin binding protein, B12-binding protein, alkaline and acid phosphatases, radioiodinated albumin and myeloma proteins, J. Gin. Invest., 37, 272, 1958.

    CAS  Google Scholar 

  123. Grossberg, A. L., Harris, E. H., and Schlamowitz, M., Enrichment and separation of alkaline phosphatase activities of human tissues by chromatography on cellulose ion-exchange absorbents, Arch. Biochem. Biophys., 93, 267, 1961.

    CAS  Google Scholar 

  124. Enström, L., Studies on calf-intestinal alkaline phosphatase. 1. Chromatographic purification, microheterogeneity and some other properties of the purified enzyme, Biochim. Biophys. Acta, 52, 36, 1961.

    Google Scholar 

  125. Landau, W., and Schlamowitz, M., Studies of factors related to the differentiation of alkaline phosphatases derived from several tissues, Arch. Biochem. Biophys., 95, 474, 1961.

    CAS  Google Scholar 

  126. Moss, D. W., Heterogeneity of human intestinal alkaline phosphatase, Nature (London), 200, 1206, 1963.

    CAS  Google Scholar 

  127. Moss, D. W., Properties of alkaline phosphatase fractions in extracts of human small intestine, Biochem. J., 94, 458, 1965.

    CAS  Google Scholar 

  128. Moog, F., Vire, H. R., and Grey, R. D., The multiple forms of alkaline phosphatase in the small intestine of the young mouse, Biochim. Biophys. Acta, 113, 336, 1966.

    CAS  Google Scholar 

  129. Butterworth, P. J., Human kidney and urinary alkaline phosphatases, Biochem. J., 107, 467, 1968.

    Google Scholar 

  130. Saini, P. K., and Done, J., Rat intestinal alkaline phosphatase: A microheterogeneous series of glycoproteins, FEBS Lett., 7, 86, 1970.

    CAS  Google Scholar 

  131. Tan, K. K., and Aw, S. E., The purification and properties of heat-stable alkaline phosphatase isoenzymes from HeLa cells, Biochim. Biophys. Acta, 235, 119, 1971.

    CAS  Google Scholar 

  132. Chang, C. H., and Moog, F., Alkaline phosphatases of the chicken duodenum. 1. Isolation and partial characterization of the multiple forms of duodenal phosphatase in the pre- and post- hatching stages, Biochim. Biophys. Acta, 258, 159, 1972.

    Google Scholar 

  133. Latner, A. L., Parsons, M., and Skillen, A. W., Isoelectric focusing of human liver alkaline phosphatase, Biochem. J., 118, 299, 1970.

    CAS  Google Scholar 

  134. Lazdunski, C., and Lazdunski, M., Les isophosphatases alcalines d’Escherichia colí: Séparation propriétés cinefiques et structurales, Biochim Biophys. Acta, 147, 280, 1967.

    CAS  Google Scholar 

  135. Davis, F. W. J., and Lees, H., Alkaline phosphatases of Neurospora crassa. Part 1, Can. J. Microbiol., 15, 455, 1969.

    CAS  Google Scholar 

  136. Harkness, D. R., Studies on human placental alkaline phosphatase. 1. Purification and crystallization, Arch. Biochem. Biophys., 126, 503, 1968.

    CAS  Google Scholar 

  137. Posen, S., Cornish, C., and Kleerekoper, M., Alkaline phosphatase and metabolic bone disorders, in: Metabolic Bone Disease (Avioli, L. V., and Krane, S. M., eds.), Vol. 1, pp. 141–148, Academic Press, New York, 1977.

    Google Scholar 

  138. Kaplan, M. M., and Righetti, A., Induction of rat liver alkaline phosphatase: The mechanism of the serum elevation in bile duct obstruction, J. Gin. Invest., 49, 508, 1970.

    CAS  Google Scholar 

  139. Etzler, M. E., and Moog, F., Immunochemical characterization by alkaline phosphatase isozymes of the young mouse duodenum, Biochim. Biophys. Acta, 154, 150, 1968.

    CAS  Google Scholar 

  140. Estborn, B., Separation of phosphatase iso-enzymes by gelfiltration, Z. Klin. Chem., 2, 53, 1964.

    CAS  Google Scholar 

  141. Dunne, J., Fennelly, J. J., and McGeeney, K., Separation of alkaline phosphatase enzymes in human serum using gel-filtration (Sephadex G200) techniques, Cancer, 20, 11, 1967.

    Google Scholar 

  142. Fennelly, J. J., Fitzgerald, M. X., and McGeeney, K., Value of differential thermostability, urea inhibition, and gel filtration of alkaline phosphatase in the identification of disease states, Gut, 10, 45, 1969.

    CAS  Google Scholar 

  143. Halford, S. E., and Schlesinger, M. J., Hybrid tetramers of alkaline phosphatase, J. Mol. Biol., 81, 261, 1973.

    CAS  Google Scholar 

  144. Shinkai, K., and Akedo, H., A multienzyme complex in serum of hepatic cancer, Cancer Res., 32, 2307, 1972.

    CAS  Google Scholar 

  145. Kyo, K., Ohira, S., Saito, T., and Nagai, A., Immunochemical analysis of macro molecular alkaline phosphatase in hepatobiliary diseases, Tohoku Univ. Res. Inst. Sci. Rep., 18, 14, 1971.

    CAS  Google Scholar 

  146. Aminoff, D., Austrius, M., and Zolfaghari, S. P., Plasma alkaline phosphatase isozymes: Isolation and characterization of isozymes, Biochim. Biophys. Acta, 242, 108, 1971.

    CAS  Google Scholar 

  147. Griffin, M. J., and Cox, R. P., Study on the mechanism of phosphatase in human cell cultures. II. Rate of enzyme synthesis and properties of base level and induced enzymes, Proc. Natl. Acad. Sci. U.S.A., 56, 946, 1966.

    CAS  Google Scholar 

  148. Moss, D. W., Immunochemical similarities between major and minor components of human placental alkaline phosphatase, Clin. Chem. Acta, 43, 447, 1973.

    Google Scholar 

  149. Smith, J. K., Eaton, R. H., Whitby, L. G., and Moss, D. W., Large-scale gel-filtration in the purification of human liver and small intestine alkaline phosphatases, Anal. Biochem., 23, 84, 1968.

    CAS  Google Scholar 

  150. Folley, S. J., and Kay, H. D., The alkaline Phosphomonoesterase of the mammary gland, Biochem. J., 29, 1837, 1935.

    CAS  Google Scholar 

  151. Asakawa, K., Über die Nierenglycerophosphatase, J. Biochem. (Tokyo), 10, 157, 1928.

    CAS  Google Scholar 

  152. Ross, M. H., Ely, J. O., and Archer, J. G., Alkaline phosphatase activity and pH optima, J. Biol. Chem., 192, 561, 1951.

    CAS  Google Scholar 

  153. Morton, R. K., The kinetics of hydrolysis of phenyl-phosphate by alkaline phosphatases, Biochem. J., 65, 674, 1957.

    CAS  Google Scholar 

  154. Motzok, I., Studies on alkaline phosphatases. 1. Kinetics of plasma phosphatase of normal and rachitic chicks, Biochem. J., 72, 169, 1959.

    CAS  Google Scholar 

  155. Motzok, I., and Branion, H. D., Studies on alkaline phosphatases. 2. Factors influencing pH optima and Michaelis constant, Biochem. J., 72, 111, 1959.

    Google Scholar 

  156. Moss, D. W., Campbell, D. M., Anagnostou-Kakaras, E., and King, E. J., Charaterisation of tissue alkaline phosphatases and their partial purification by starch-gel electrophoresis, Biochem. J., 81, 441, 1961.

    CAS  Google Scholar 

  157. Moss, D. W., Campbell, D. M., Anagnostou-Kakaras, E., and King, E. J., Separation and characterisation of alkaline phosphatase isoenzymes from blood and other tissues, Pure Appl Chem., 3, 397, 1961.

    CAS  Google Scholar 

  158. Eaton, R. H., and Moss, D. W., Partial purification and some properties of human bone alkaline phosphatase, Enzymologia 35, 31, 1968.

    CAS  Google Scholar 

  159. Scutt, P. B., and Moss, D. W., Reversible inactivation of alkaline phosphatase in acid solution, Enzymologia, 35, 157, 1968.

    CAS  Google Scholar 

  160. Price, C. P., Hill, P. G., and Sammons, H. G., The nature of the alkaline phosphatases of bile, J. Gin. Pathol., 25, 149, 1972.

    CAS  Google Scholar 

  161. Eaton, R. H., and Moss, D. W., Kinetic studies on the orthophosphatase and inorganic pyrophosphatase activities of human alkaline phosphatases, Enzymologia, 35, 168, 1968.

    CAS  Google Scholar 

  162. McCoy, E. E., Park, J., and England, J., A fluorometric assay and properties of leucocyte alkaline phosphatase, Clin. Chim. Acta, 12, 453, 1965.

    CAS  Google Scholar 

  163. Morris, H., Studies on the relationship between the isozymes of alkaline phosphatase from Escherichia coli, Ph.D. thesis, University of Sydney, Australia, 1970.

    Google Scholar 

  164. Ahmed, Z., and King, E. J., Kinetics of placental alkaline phosphatase, Biochim. Biophys. Acta, 45, 581, 1960.

    CAS  Google Scholar 

  165. Birkett, D. J., Conyers, R. A. J., Neale, F. C., Posen, S., and Brudenell-Woods, J., Action of urea on human alkaline phosphatases: With a description of some automated techniques for the study of enzyme kinetics, Arch. Biochem. Biophys., 121, 470, 1967.

    CAS  Google Scholar 

  166. Richter, J., and Ohlen, J., Vergleichende Untersuchungen zur katalytischen Aktivität der alkalischen Phosphatase unter Testbedingungen, Z. Klin. Giern. Klin. Biochem., 12, 432, 1974.

    CAS  Google Scholar 

  167. Van Belle, H., Kinetics and inhibition of alkaline phosphatases from canine tissues, Biochim. Biophys. Acta, 289, 158, 1972.

    Google Scholar 

  168. Le Hégarat, J. C., and Anagnostopoulos, C., Purification, subunit structure and properties of two repressible phosphohydrolases of Bacillus subtilis, Eur. J. Biochem, 39, 525, 1973.

    Google Scholar 

  169. Heppel, L. A., Harkness, D. R., and Hilmoe, R. J., A study of the substrate specificity and other properties of the alkaline phosphatase of Escherichia coli, J. Biol Chem., 237, 841, 1962.

    CAS  Google Scholar 

  170. Simpson, R. T., and Vallee, B. L., Negative homotropic interactions in binding of substrate to alkaline phosphatase of Escherichia coli, Biochemistry, 9, 953, 1970.

    CAS  Google Scholar 

  171. Hinberg, I., and Laidler, K. J., Influence of pH on the kinetics of reactions catalyzed by alkaline phosphatase, Can. J. Biochem., 51, 1096, 1973.

    CAS  Google Scholar 

  172. Halford, S. E., Lennette, D. A., and Schlesinger, M. J., A mutationally altered alkaline phosphatase from Escherichia coli II. Structural and catalytic properties of the activated enzyme, J. Biol. Chem., 247, 2095, 1972.

    CAS  Google Scholar 

  173. Waight, R. D., Leff, P., and Bardsley, W. G., Steady-state kinetic studies of the negative cooperativity and flip-flop mechanism for Escherichia coli alkaline phosphatase, Biochem. J., 167, 787, 1977.

    CAS  Google Scholar 

  174. Aebi, H., Vergleichende Untersuchungen über die Aktivität, Magnesium-Aktivierung und Stabilität der alkalischen Nierenphosphatase, Helv. Chim. Acta, 32, 464, 1949.

    CAS  Google Scholar 

  175. Gryder, R. M., Friedenwald, J. S., and Carlson, C., The two alkaline phosphatases for glycerophosphate in the rat’s kidney, Arch. Biochem. Biophys., 54, 281, 1955.

    CAS  Google Scholar 

  176. Wilson, I. B., Dayan, J., and Cyr, K., Some properties of alkaline phosphatase from Escherichia coli: Transphosphorylation, J. Biol. Chem., 239, 4182, 1964.

    CAS  Google Scholar 

  177. Dayan, J., and Wilson, I. B., The phosphorylation of Tris by alkaline phosphatase, Biochim. Biophys. Acta, 81, 620, 1964.

    CAS  Google Scholar 

  178. Chappelet-Tordo, D., Fosset, M., Iwatsubo, M., Gache, C., and Lazdunski, M., Intestinal alkaline phosphatase: Catalytic properties and half of the sites reactivity, Biochemistry, 13, 1788, 1974.

    CAS  Google Scholar 

  179. McComb, R. B., and Bowers, G. N., Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum, Clin. Chem., 18, 97, 1972.

    CAS  Google Scholar 

  180. Delory, G. E., and King, E. J., The rat of enzymic hydrolysis of phosphoric esters. 2. Relation of structure to dissociation constant, Michaelis constant and rate of hydrolysis, Biochem. J., 37, 547, 1943.

    CAS  Google Scholar 

  181. Haije, W. G., Influence of buffer conditions on the activities of some isoenzymes of alkaline phosphatase in the serum, Clin. Chim. Acta, 98, 23, 1973.

    Google Scholar 

  182. McComb, R. B., Unpublished observations, 1976.

    Google Scholar 

  183. Whitaker, K. B., and Moss, D. W., A comparison of the transphosphorylating activities of human liver and intestinal alkaline phosphatases, Clin. Chim. Acta, 52, 347, 1974.

    CAS  Google Scholar 

  184. Amador, E., and Urban, J., Transphosphorylation by human alkaline phosphatases, Am. J. Gin. Pathol., 57, 167, 1972.

    CAS  Google Scholar 

  185. Motzok, I., and Branion, H. D., Studies on alkaline phosphatases. 3. Influence of age of fowl and mammals on pH optima, Biochem. J., 80, 5, 1961.

    CAS  Google Scholar 

  186. Motzok, I., Studies on alkaline phosphatases. 4. Influence of dietary minerals on pH optima and reaction volocities in the fowl, Biochem. J., 87, 172, 1963.

    CAS  Google Scholar 

  187. Aebi, H., and Abelin, I., Die Wirkungsweise verschiedener Effektoren auf die Aktivität der alkalischen Nierenphosphatase (Magnesium, Mangan, Na-Carbonat-Hydrogen-carbonat, Ammonium- Ionen und Aminosäuren), Helv. Chim. Acta, 31, 1943, 1948.

    CAS  Google Scholar 

  188. Grier, R. S., Hood, M. B., and Hoagland, M. B., Observations on the effects of beryllium on alkaline phosphatase, J. Biol. Chem., 180, 289, 1949.

    CAS  Google Scholar 

  189. Posen, S. P., Unpublished observations, 1969.

    Google Scholar 

  190. Bodansky, O., and Bakwin, H., The phosphatase hydrolysis of diphospho-l-glyeerie acid, J. Biol. Chem., 104, 747, 1934.

    CAS  Google Scholar 

  191. Morton, R. K., Some properties of alkaline phosphatase of cows milk and calf intestinal mucosa, Biochem. J., 60, 573, 1955.

    CAS  Google Scholar 

  192. Utida, S., Oide, M., and Oide, H., Ionic effects on alkaline phosphatase activity in intestinal mucosa with special reference to sea-water adaptation of the Japanese eel Anguilla japonica, Comp. Biochem. Physiol., 27, 239, 1968.

    CAS  Google Scholar 

  193. Oide, M., Purification and some properties of alkaline phosphatase from intestinal mucosa of the eel adapted to fresh water or sea water, Comp. Biochem. Physiol., 36, 241, 1970.

    CAS  Google Scholar 

  194. Whitmore, D. H., and Goldberg, E., Trout intestinal alkaline phosphatases. 1. Some physical- chemical characteristics, J. Exp. Zool., 182, 47, 1972.

    CAS  Google Scholar 

  195. Nose, K., Takaoka, T., and Katsuda, H., Two different activities of alkaline phosphatase in cultured mammalian cells, Arch. Biochem. Biophys., 155, 1, 1973.

    CAS  Google Scholar 

  196. Posen, S., Unpublished observations, 1971.

    Google Scholar 

  197. Robison, R., The possible significance of hexose-phosphoric esters in ossification, Biochem. J., 17, 286, 1923.

    CAS  Google Scholar 

  198. King, E. J., and Armstrong, A. R., A convenient method for determining serum and bile phosphatase activity, Can. Med. Assoc. J., 31, 376, 1934.

    CAS  Google Scholar 

  199. Bessey, O. A., Lowry, O. H., and Brock, M. J., A method for the rapid determination of alkaline phosphatase with five cubic millimeters of serum, J. Biol. Chem., 164, 321, 1946.

    CAS  Google Scholar 

  200. Tsou, K. C., and Su, H. C. F., A new colorimetric method for the determination of alkaline phosphatase with indoxyl phosphate, Anal. Biochem., 11, 54, 1965.

    CAS  Google Scholar 

  201. Fernley, H. N., and Walker, P. G., Kinetic behaviour of calf-intestinal alkaline phosphatase with 4-methyl-umbelliferyl phosphate, Biochem. J., 97, 95, 1965.

    CAS  Google Scholar 

  202. Fishman, W. H., Green, S., and Inglis, N., Organ-specific behavior exhibited by rat intestine and liver alkaline phosphatase, Biochim. Biophys. Acta, 62, 363, 1962.

    CAS  Google Scholar 

  203. Herlant, M., and Timiras, P. S., Alkaline phosphatases in various tissues of the rat during the alarm reaction, Endocrinology, 48, 243, 1950.

    Google Scholar 

  204. Pitkanen, E., The pyrophosphatase activity in human blood serum, Scand. J. Gin. Lab. Invest., 12, 143, 1960.

    CAS  Google Scholar 

  205. Keiding, N. R., Intestinal alkaline phosphatase in human lymph and serum, Scand. J. Gin. Lab. Invest., 18, 134, 1966.

    CAS  Google Scholar 

  206. Wolf, M., Dinwoodie, A., and Morgan, H. G., Comparison of alkaline phosphatase isoenzymes activity using five standard methods, Clin. Giim. Acta, 24, 131, 1969.

    CAS  Google Scholar 

  207. Moss, D. W., Determination of intestinal alkaline phosphatase in serum by substrate-specificity measurements, Clin. Chim. Acta, 35, 413, 1971.

    CAS  Google Scholar 

  208. Moog, F., The functional differentiation of the small intestine. VIII. Regional differences in the alkaline phosphatases of the small intestine of the mouse from birth to one year, Dev. Biol., 3, 153, 1961.

    CAS  Google Scholar 

  209. Moog, F., Etzler, M. E., and Grey, R. D., The differentiation of alkaline phosphatase in the small intestine, Ann. N. Y. Acad. Sci., 166, 447, 1969.

    CAS  Google Scholar 

  210. Zittle, C. A., and Bingham, E. W., Reactivity of the alkaline phosphatases of bovine milk and intestinal mucosa with the substrates phenyl phosphate and o-carboxyphenyl phosphate, Arch. Biochem. Biophys., 86, 25, 1960.

    CAS  Google Scholar 

  211. Fernley, H. N., Thiophosphorylation of alkaline phosphatase, Nature (London) New Biol., 241, 110, 1973.

    CAS  Google Scholar 

  212. Ghosh, B. K., Wouters, J. T. M., and Lampen, J. O., Distribution of the sites of alkaline phosphatase(s) activity in vegetative cells of Bacillus subtilis, J. Bacteriol., 108, 928, 1971.

    CAS  Google Scholar 

  213. Cornish, C. J., Neale, F. C., and Posen, S., An automated fluorometric alkaline phosphatase micro-assay with 4-methylumbelliferyl phosphate as a substrate, Am. J. Gin. Pathol., 53, 68, 1970.

    CAS  Google Scholar 

  214. Schwartz, M. K., Kessler, G., and Bodansky, O., Comparison of serum alkaline phosphatase activities determined with sodium beta glycerophosphate and sodium phenylphosphate as substrates, Am. J. Gin. Pathol., 33, 275, 1960.

    CAS  Google Scholar 

  215. Deren, J. J., Williams, L. A., Muench, H., Chalmers, T., and Zamchek, N., Comparative study of four methods of determining alkaline phosphatase, N. Engl. J. Med., 270, 1277, 1964.

    CAS  Google Scholar 

  216. Tietz, N. W., Woodrow, D., and Woodrow, B., A comparative study of the Bodansky and the Bessey, Lowry and Brock methods for alkaline phosphatase in serum, Clin. Chim. Acta, 15, 365, 1967.

    CAS  Google Scholar 

  217. Healy, P. J., Serum alkaline phosphatase activity in cattle, Clin. Chim. Acta, 33, 423, 1971.

    CAS  Google Scholar 

  218. Bell, D. J., Tissue components of the domestic fowl. 4. Plasma alkaline phosphatase activity, Biochem. J., 75, 224, 1960.

    CAS  Google Scholar 

  219. Alcock, N. W., and Shils, M. E., Association of inorganic pyrophosphatase activity with normal calcification of rat costal cartilage in vivo, Biochem. J., 112, 505, 1969.

    Google Scholar 

  220. Cox, R. P., Gilbert, P., and Griffin, M. S., Alkaline inorganic pyrophosphatase activity of mammalian-cell alkaline phosphatase, Biochem. J., 105, 155, 1967.

    CAS  Google Scholar 

  221. Moss, D. W., Eaton, R. H., Smith, J. K., and Whitby, L. G„ Association of inorganic-pyrophosphatase activity with human alkaline phosphatase preparations, Biochem. J., 102, 53, 1967.

    CAS  Google Scholar 

  222. Eaton, R. H., and Moss, D. W., Alkaline orthophosphatase and inorganic pyrophosphatase activities in human serum, Nature (London), 214, 842, 1967.

    CAS  Google Scholar 

  223. Eaton, R. H., and Moss, D. W., Inhibition of the orthophosphatase and pyrophosphatase activities of human alkaline-phosphatase preparations, Biochem. J., 102, 917, 1967.

    CAS  Google Scholar 

  224. Eaton, R. H., and Moss, D. W., Organic pyrophosphates as substrates for human alkaline phos¬phatases, Biochem. J., 105, 1307, 1967.

    CAS  Google Scholar 

  225. Lieberherr, M., Vreven, J., and Vaes, G., The acid and alkaline phosphatases, inorganic pyrophosphatases and phosphoprotein phosphatase of bone. 1. Characterization and assay, Biochim. Biophys. Acta, 293, 160, 1973.

    CAS  Google Scholar 

  226. Fernley, H. N., and Walker, P. G., Studies on alkaline phosphatase: Inhibition by phosphate derivatives and the substrate specificity, Biochem. J., 104, 104, 1967.

    Google Scholar 

  227. Butterworth, P. J., The pyrophosphatase activity of pig kidney alkaline phosphatase and its inhibition by magnesium ions and excess of pyrophosphate, Biochem. J., 110, 671, 1968.

    CAS  Google Scholar 

  228. Hørder, M., Inorganic pyrophosphate-phosphohydrolytic activity associated with human placental alkaline orthophosphatase: Nature of substrate and role of magnesium, Biochim. Biophys. Acta, 341, 41, 1914.

    Google Scholar 

  229. Kuhlman, R. E., Phosphatases in epiphyseal cartilage: Their possible role in tissue synthesis, J. Bone Joint Surg., 47A, 545, 1965.

    CAS  Google Scholar 

  230. Lysloff-Skipski, I. A., and Monder, C. A., Separation of inorganic pyrophosphatase and alkaline phosphatase of calcifying rat costal cartilage, Abstract No. 159, presented to the 162nd National Meeting, American Chemical Society, 1972.

    Google Scholar 

  231. Hørder, M., Enzyme catalyzed hydrolysis of inorganic pyrophosphate, Enzyme 19, 165, 1975.

    Google Scholar 

  232. Hørder, M., Inorganic pyrophosphatase activity in human sera with elevated alkaline orthophosphatase activity, Clin. Chim. Acta, 42, 373, 1972.

    Google Scholar 

  233. Hørder, M., The inorganic pyrophosphatase activity associated with forms of alkaline phosphatases isolated from human serum, Clin. Chim. Acta, 49, 383, 1973.

    Google Scholar 

  234. Plocke, D. J., and Vallee, B. L., Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents, Biochemistry, 1, 1039, 1962.

    CAS  Google Scholar 

  235. Hayashi, M., Unemoto, T., and Hayashi, M., pH- and anion-dependent salt modifications of alkaline phosphatase from a slightly halophilic Vibrio alginolyticus, Biochim. Biophys. Acta, 315, 83, 1973.

    CAS  Google Scholar 

  236. Schlamowitz, M., Production of antibodies against dog intestinal phosphatase, J. Biol. Chem., 206, 361, 1954.

    CAS  Google Scholar 

  237. Schlamowitz, M., Specificity of dog intestinal phosphatase antiserum, J. Biol. Chem., 206, 369, 1954.

    CAS  Google Scholar 

  238. Schlamowitz, M., and Bodansky, 0., Tissue sources of human serum alkaline phosphatase as determined by immunochemical procedures, J. Biol. Chem., 234, 1433, 1959.

    CAS  Google Scholar 

  239. Moog, F., and Angeletti, P. U., Immunological difference between duodenal and jejunal phosphatase of the mouse, Biochim. Biophys. Acta, 60, 440, 1962.

    CAS  Google Scholar 

  240. Korngold, L., The antigenic properties of alkaline phosphatase of human kidney, kidney tumors and urine, Int. Arch. Allergy, 37, 366, 1970.

    CAS  Google Scholar 

  241. Birkett, D. J., Done, J., Neale, F. C., and Posen, S., Serum alkaline phosphatase in pregnancy: An immunological study, Br. Med. J., 1, 1210, 1966.

    CAS  Google Scholar 

  242. Usategui-Gomez, M., Yeager, F. M., and Fernandez de Castro, A., The use of polymerized antisera for the determination of human placental alkaline phosphatase in pregnancy sera, Clin. Chim. Acta, 46, 355, 1973.

    CAS  Google Scholar 

  243. Usategui-Gomez, M., Yeager, F. M., and Fernandez de Castro, A., A sensitive immunochemical method for the determination of the Regan isoenzyme in serum, Cancer Res., 33, 1574, 1973.

    Google Scholar 

  244. Kleerekoper, M., Home, M., Cornish, C. J., and Posen, S., Serum alkaline phosphatase after fat ingestion, Clin. Sci., 38, 339, 1970.

    CAS  Google Scholar 

  245. Sussman, H. H., Evidence that the increased serum alkaline phosphatase activity in patients with osteomalacia or Paget’s disease is from liver phosphatase isoenzyme, Clin. Res., 16, 130, 1968.

    Google Scholar 

  246. Beckman, G., Beckman, L., and Lundgren, E., Isozyme variations in human cells grown in vitro. IV. Identity between alkaline phosphatases from Hela cells and placenta?, Hum. Hered., 20, 182, 1970.

    CAS  Google Scholar 

  247. Fishman, L., Inglis, N. R., and Fishman, W. H., Preparation and characterization of human intestinal alkaline phosphatase antigen, Clin. Chim. Acta, 38, IS, 1911.

    Google Scholar 

  248. Inglis, N. R., Fishman, L., Stolbach, L. L., Warshaw, J. B., and Fishman, W. H., A comparison of chyle isoenzymes of alkaline phosphatase in chyle and hypophosphatasemic sera, Clin. Chim. Acta, 38, 61, 1912.

    Google Scholar 

  249. Cocks, G. T., and Wilson, A. C., Immunological detection of single amino acid substitutions in alkaline phosphatase, Science, 164, 188, 1969.

    CAS  Google Scholar 

  250. Schlesinger, M. J., The reversible dissociation of the alkaline phosphatase of Escherichia coli, J. Biol. Chem., 242, 1599, 1967.

    CAS  Google Scholar 

  251. Tammann, G., Zur Wirkung ungeformter Fermente, Z. Physiol. Chem., 18, 426, 1895.

    Google Scholar 

  252. Lustig, V., and Kellen, J. A., Temperature optimum of alkaline phosphatases in some homeothermic and Poikilothermie species, Comp. Biochem. Physiol., 39B, 311, 1971.

    CAS  Google Scholar 

  253. Whitmore, D. H., and Goldberg, E., Trout intestinal alkaline phosphatases. II. The effect of temperature upon enzymic activity in vitro and in vivo, J. Exp. Zool., 182, 59, 1972.

    CAS  Google Scholar 

  254. Cowling, F. M., Purification and characterization of alkaline phosphatase of Bacillus licheniformis,Diss. Abstr.,30,1260-B, 1969.

    Google Scholar 

  255. Moelwyn-Hughes, E. A., The kinetics of enzyme reactions, Ergeb. Enzymforsch., 2, 1, 1933.

    CAS  Google Scholar 

  256. Stearn, A. E., The theory of absolute reaction rates applied to enzyme catalysis, Ergeb. Enzym- forsch., 7, 1, 1937.

    Google Scholar 

  257. Sizer, I. W., Effects of temperature on enzyme kinetics, in: Advances in Enzymology, Vol. 3 (Nord, F. F., and Werkman, C. H., eds.), p. 35, Interscience, New York, 1943.

    Google Scholar 

  258. Kavanau, J. L., Enzyme kinetics and the rate of biological processes, J. Gen. Physiol., 34, 193, 1951.

    Google Scholar 

  259. Lauffer, M. A., and Price, W. C., Thermal denaturation of tobacco mosaic virus, J. Biol. Chem., 133, 1, 1940.

    CAS  Google Scholar 

  260. Kauzmann, W., Some factors in the interpretation of protein denaturation, Adv. Protein Chem., 14, 1, 1959.

    CAS  Google Scholar 

  261. Chick, H., and Martin, C. J., On the “heat coagulation” of proteins, J. Physiol., 40, 404, 1910.

    CAS  Google Scholar 

  262. Goldstein, A., and Doherty, M. E., Properties and behaviour or purified human plasma Cholinesterase. 1. Stability and thermal denaturation, Arch. Biochem. Biophys., 33, 22, 1951.

    CAS  Google Scholar 

  263. Rowland, S. J., The heat denaturation of albumin and globulin in milk, J. Dairy Res., 5, 46, 1933.

    CAS  Google Scholar 

  264. Straub, F. B., Formation of the secondary and tertiary structure of enzymes, Adv. Enzymol., 26, 89, 1964.

    Google Scholar 

  265. Allen, M. B., The dynamic nature of thermophily, J. Gen Physiol., 33, 205, 1950.

    CAS  Google Scholar 

  266. Wisdom, C., and Welker, N. E., Membranes of Bacillus stearothermophilus: Factors affecting protoplast stability and thermostability of alkaline phosphatase and reduced nicotinamide adenine dinucleotide oxidase, J. Bacteriol., 114, 1336, 1973.

    CAS  Google Scholar 

  267. Militzer, W., and Burns, L., Thermal enzymes. VI. Heat stability of pyruvic oxidase, Arch. Biochem. Biophys., 52, 66, 1954.

    CAS  Google Scholar 

  268. Jenkins, W. T., Yphantis, D. A., and Sizer, I. W., Glutamic aspartic transaminase, J. Biol. Chem., 234, 51, 1959.

    CAS  Google Scholar 

  269. Okunuki, K., Denaturation and inactivation of enzyme proteins, Adv. Enzymol., 23, 29, 1961.

    CAS  Google Scholar 

  270. Posen, S., Studies in human alkaline phosphatases, M.D. thesis, University of Adelaide, Australia, 1966.

    Google Scholar 

  271. Eyring, H., and Stearn, A. E., The application of the theory of absolute reaction rates to proteins, Chem. Rev., 24, 253, 1939.

    CAS  Google Scholar 

  272. Moss, D. W., Shakespeare, M. J., and Thomas, D. M., Observations on the heat-stability of alkaline phosphatase isoenzymes in serum, Clin. Chim. Acta, 40, 35, 1972.

    CAS  Google Scholar 

  273. Yunis, A. A., and Gentry, M. A., Purification and properties of alkaline phosphatase from rat chloroma, Cancer Res., 31, 39, 1971.

    CAS  Google Scholar 

  274. Adler, L., Über die Phosphatasen im Malz, Biochem. Z., 70, 1, 1915.

    CAS  Google Scholar 

  275. Demuth, F., Über Phosphatstoffwechsel. 1. Mitteilung. Über Hexosephosphatasen in menschlichen Organen und Körperflüssigkeiten, Biochem. Z., 159, 415, 1925.

    CAS  Google Scholar 

  276. Umeno, M., Studien über Phosphatase. IV. Mitteilung. Über die optimale und die Zerstörungtemperatur der Nierenphosphatase, Biochem. Z., 231, 334, 1931.

    CAS  Google Scholar 

  277. Köster, L., The presence of glycerophosphatase in human faeces, Acta Med. Scand., 101, 482, 1939.

    Google Scholar 

  278. Graham, W. R., and Kay, H. D., Phosphorus compounds of milk. V. The phosphorus partition in milk with preliminary observations on milk phosphatase, J. Dairy Res., 5, 54, 1933.

    Google Scholar 

  279. Jacobsen, E., Studien über die Stabilität und Trennbarkeit einiger Phosphatasen, Biochem. Z., 263, 302, 1933.

    CAS  Google Scholar 

  280. Kay, H. D., and Graham, W. R., Phosphorus compounds of milk. VI. The effect of heat on milk phosphatase: A simple method for distinguishing raw from pasteurised milk, raw from pasteurised cream and butter made from raw cream from that made from pasteurised cream, J. Dairy Res., 5, 63, 1933.

    CAS  Google Scholar 

  281. Kay, H. D., and Graham, W. R., The phosphatase test for pasteurised milk, J. Dairy Res.,(5, 191, 1935.

    Google Scholar 

  282. Morton, R. K., The lipoprotein particles in cow’s milk, Biochem., J., 57, 231, 1954.

    CAS  Google Scholar 

  283. Gomori, G., The distribution of phosphatase in normal organs and tissues, J. Cell. Comp. Physiol., 17, 71, 1941.

    CAS  Google Scholar 

  284. Kugler, O. E., Histochemical localisation of alkaline phosphatase and nucleic acids in the oocytes of the bluegill Lepomis machochirus (Refinesque), J. Histochem. Cytochem., 1, 296, 1953.

    CAS  Google Scholar 

  285. Posen, S., Unpublished observations, 1972.

    Google Scholar 

  286. Bodansky, O., The energy of activation of the hydrolysis of sodium beta-glycerophosphate by bone phosphatase at optimal pH, J. Biol. Chem., 129, 197, 1939.

    CAS  Google Scholar 

  287. Wallach, D. P., and Ko, H., Some properties of an alkaline phosphatase from rat adipose tissue, Can. J. Biochem., 42, 1445, 1964.

    CAS  Google Scholar 

  288. Licht, P., The temperature dependence of myosin adenosine triphosphatase and alkaline phosphatase in lizaids, Comp. Biochem. Physiol., 12, 331, 1964.

    CAS  Google Scholar 

  289. Nagode, L. A., Koestner, A., and Steinmeyer, C. L., The effects of purification and serum proteins on the organ-identifying properties of alkaline phosphatases from canine tissues, Clin. Chim. Acta, 26, 55, 1969.

    CAS  Google Scholar 

  290. Garen, A., and Levinthal, C., A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli, Biochim. Biophys. Acta, 38, 470, 1960.

    CAS  Google Scholar 

  291. Garen, A., and Garen, S., Complementation in vivo between structural mutants of alkaline phosphatase from E. coli, J. Mol. Biol., 7, 13, 1963.

    CAS  Google Scholar 

  292. Brown, D. K., Militzer, W., and Georgi, C. E., The effect of growth temperature on the heat stability of abacterial pyrophosphatase, Arch. Biochem. Biophys., 70, 248, 1957.

    CAS  Google Scholar 

  293. Nitowsky, H. M., and Herz, F., Hormonal regulation of alkaline phosphatase in dispersed cell cultures, Biochem. Biophys. Res. Commun., 11, 261, 1963.

    CAS  Google Scholar 

  294. Herz, F., Kaplan, E., and Fineman, E. L., Regulation of alkaline phosphatase activity in KB cells: Influence of serum, Biochim. Biophys. Acta, 304, 660, 1973.

    CAS  Google Scholar 

  295. Neale, F. C., Clubb, J. S., Hotchkis, D., and Posen, S., The heat stability of human placental alkaline phosphatase, J. Clin. Pathol., 18, 359, 1965.

    CAS  Google Scholar 

  296. Harkness, D. R., Studies on human placental alkaline phosphatase. 2. Kinetic properties and studies on the apoenzyme, Arch. Biochem. Biophys., 126, 513, 1968.

    CAS  Google Scholar 

  297. Neale, F. C., Clubb, J. S., and Posen, S., Artificial elevation of serum alkaline phosphatase concentration, Med. J. Aust., 2, 684, 1963.

    Google Scholar 

  298. Clubb, J. S., Neale, F. C., and Posen, S., The behavior of infused placental alkaline phosphatase in human subjects, J. Lab. Clin. Med., 66, 493, 1965.

    CAS  Google Scholar 

  299. Mackie, J. A., Arvan, D. A., Mullen, J. L., and Rawnsley, H. M., Elevated serum alkaline phosphatase levels after the administration of certain preparations of human albumin, Am. J. Surg., 121, 57, 1971.

    Google Scholar 

  300. Manning, J. P., Inglis, N. R., Green, S., and Fishman, W. H., Characterization of placental alkaline phosphatase from three primates: African green and rhesus monkey and baboon, Enzymologia, 37, 251, 1969.

    CAS  Google Scholar 

  301. Leroux, M. L., and Perry, W. F., Some characteristics of placental alkaline phosphatase of a variety of mammals, Enzymologia 41, 241, 1911.

    Google Scholar 

  302. Hindriks, F. R., Groen, A., and Kroon, A. M., On the relation of heavy metals to the activity and heat stability of alkaline phosphatase from human placenta, Biochim. Biophys. Acta, 315, 94, 1973.

    CAS  Google Scholar 

  303. Posen, S., Neale, F. C., and Clubb, J. S., Heat inactivation in the study of human alkaline phosphatases, Ann. Int. Med., 62, 1234, 1965.

    CAS  Google Scholar 

  304. Fishman, W. H., Inglis, N. R., Green, S., Anstiss, C. L., Gosh, N. K., Reif, A. E., Rustigian, R., Krant, M. J., and Stolbach, L. L., Immunology and biochemistry of Regan isoenzyme of alkaline phosphatase in human cancer, Nature (London), 219, 697, 1968.

    CAS  Google Scholar 

  305. Stolbach, L. L., Krant, M. J., and Fishman, W. H., Ectopic production of an alkaline phosphatase isoenzyme in patients with cancer, N. Engl. J. Med., 281, 757, 1969.

    CAS  Google Scholar 

  306. Jacoby, B., and Bagshawe, K. D., Placental-type alkaline phosphatase from human tumour tissue, Clin. Chim. Acta, 35, 473, 1971.

    CAS  Google Scholar 

  307. Romslo, I., Bjark, P., and Solberg, C.0., Ectopic alkaline phosphatase production in metastasizing ventricular carcinoma, Scand. J. Clin. Lab. Invest., 28, 21, 1971.

    CAS  Google Scholar 

  308. Warnes, T. W., Timperley, W. R., Hine, P., and Kay, G., Pancreatic alkaline phosphatase and a tumour variant, Gut, 13, 513, 1972.

    CAS  Google Scholar 

  309. Kadlecova, L., and Stepan, J., Phosphatases. VI. pH dependence of the organ-specific thermostability of alkaline phosphatase in tissue homogenates, Experientia, 28, 1284, 1972.

    CAS  Google Scholar 

  310. Healy, P. J., Serum alkaline phosphatase activity in sheep, Aust. J. Exp. Biol. Med. Sci., 52, 375, 1974.

    CAS  Google Scholar 

  311. Melnykovych, G., and Sylber, C. K., Effects of cations on activity and thermostability of alkaline phosphatase in Hela cells, Proc. Soc. Exp. Biol. Med., 121, 165, 1966.

    CAS  Google Scholar 

  312. Lustig, V., and Kellen, J. A., The ultrastructural localization of alkaline phosphatase isoenzymes in some normal and malignant cells, Enzyme, 12, 76, 1971.

    CAS  Google Scholar 

  313. Butterworth, P. J., and Moss, D. W., The effect of urea on human alkaline phosphatase preparations, Enzymologia, 32, 269, 1967.

    CAS  Google Scholar 

  314. Bahr, M., and Wilkinson, J. H., Urea as a selective inhibitor of human tissue alkaline phosphatase, Clin. Chim. Acta, 17, 367, 1967.

    CAS  Google Scholar 

  315. Dyck, W. P., Hall, F. F., and Ratcliff, C. R., Hormonal control of intestinal alkaline phosphatase secretion in the dog, Gastroenterology, 65, 445, 1973.

    CAS  Google Scholar 

  316. Trubowitz, S., Feldman, D., Morgenstern, S. W., and Hunt, V. M., The isolation, purification and some properties of the alkaline phosphatase of human leukocytes, Biochem. J., 80, 369, 1961.

    CAS  Google Scholar 

  317. Plocke, D. J., Levinthal, C., and Vallee, B., Alkaline phosphatase of Escherichia coli: A zinc metalloenzyme, Biochemistry, 1, 373, 1962.

    CAS  Google Scholar 

  318. Cloetens, R., Reversible Abspaltung des zweiten Metalles der alkalischen Phosphatase II, Biochem. Z., 308, 31, 1941.

    Google Scholar 

  319. Drill, V. A., Annegers, J. H., and Ivy, A. C., Effect of cyanide, fluoride and magnesium on serum phosphatase activity during hepatic damage, J. Biol. Chem., 152, 339, 1944.

    CAS  Google Scholar 

  320. Drill, V. A., and Riggs, D. S., Inhibition of alkaline serum phosphatase activity during liver disease, J. Biol. Chem., 162, 21, 1946.

    CAS  Google Scholar 

  321. Bodansky, O., Mechanism of inhibition of phosphatase activity by glycine, J. Biol. Chem., 165, 605, 1946.

    CAS  Google Scholar 

  322. Anderson, R. A., Bosron, W. F., Kennedy, F. S., and Vallee, B. L., Role of magnesium in Escherichia coli alkaline phosphatase, Proc. Natl. Acad. Sci. U.S.A., 72, 2989, 1975.

    CAS  Google Scholar 

  323. Portmann, P., Zur Kenntnis der alkalischen Darmphosphatase, Z. Physiol. Chem., 309, 87, 1957.

    CAS  Google Scholar 

  324. Conyers, R. A. J., Birkett, D. J., Neale, F. C., Posen, S., and Brudenell-Woods, J., The action of EDTA on human alkaline phosphatases, Biochim. Biophys. Acta, 139, 363, 1967.

    CAS  Google Scholar 

  325. Dabich, D., and Neuhaus, O. W., Purification and properties of bovine synovial fluid alkaline phosphatase, J. Biol. Chem., 241, 415, 1966.

    CAS  Google Scholar 

  326. Moreno, J., Asteggiano, C. A., De Cattoni, S. D., and Blanco, A., Intestinal alkaline phosphatase: Qualitative changes produced by deficient diet in rats, Metabolism 21, 513, 1972.

    CAS  Google Scholar 

  327. Agus, S. G., Cox, R. P., and Griffin, M. J., Inhibition of alkaline phosphatase by cysteine and its analogues, Biochim. Biophys. Acta, 118, 363, 1966.

    CAS  Google Scholar 

  328. Simpson, R. T., and Vallee, B. L., Zinc and cobalt alkaline phosphatase, Ann. N. Y. Acad. Sci., 166, 670, 1969.

    CAS  Google Scholar 

  329. Lazdunski, C., Petitclerc, C. Chappelet, D., and Lazdunski, M., On the mechanism of the Zn2+ and Co2+-alkaline phosphatases of E. coli: Number of sites and anticooperativity, Biochem. Biophys. Res. Commun., 37, 744, 1969.

    CAS  Google Scholar 

  330. Cox, R. P., Elson, N. A., Tu, S. H., and Griffin, M. J., Hormonal induction of alkaline phosphatase by an increase in catalytic efficiency of the enzyme, J. Mol. Biol. 58, 197, 1971.

    CAS  Google Scholar 

  331. Albers, D., Beeinflussung der Phosphatase verschiedener Reinheitsgraden durch U.V. und Roentgenstrahlen, Biochem. Z., 306, 143, 1940.

    CAS  Google Scholar 

  332. McLaren, A. D., Luse, R. A., and Skujins, J. J., Sterilisation of soil by irradiation and some further observations on soil enzyme activity, Proc. Am. Soc. Soil Sci., 26, 371, 1962.

    CAS  Google Scholar 

  333. Skujins, J. J., Braal, L., and McLaren, A. D., Characterisation of phosphatase in a terrestial soil sterilised with an electron beam, Enzymologia, 25, 125, 1962.

    CAS  Google Scholar 

  334. Bamann, E., and Diederichs, K., Trennung der beiden isodynamen Phospho-esterasen tierischer Organe durch ein selektives Inaktivierungs-Verfahren (III. Abhandlung Zur Kenntnis der Phosphatasen), Ber. Dtsch. Chem. Ges. B, 67, 2019, 1934.

    Google Scholar 

  335. Cloetens, R., Préparation et propriétés de la phosphatase “Alcaline” I, Enzymologia, 7, 157, 1939.

    CAS  Google Scholar 

  336. Butterworth, P. J., The reversible inactivation of pig kidney alkaline phosphatase at low pH, Biochem. J., 108, 243, 1968.

    CAS  Google Scholar 

  337. Barman, T. E., and Gutfreund, H., The catalytic-centre activity and kinetic properties of bovine milk alkaline phosphatase, Biochem. J., 101, 460, 1966.

    CAS  Google Scholar 

  338. Carey, M. J., and Butterworth, P. J., The action of cyanate on human and pig kidney alkaline phosphatases, Biochem. J., 111, 745, 1969.

    CAS  Google Scholar 

  339. Fishman, W. H., and Kreisher, J. H., Stereospecific, organ-specific inhibition of intestinal alkaline phosphatase, Ann. N. Y. Acad. Sci., 103, 951, 1963.

    Google Scholar 

  340. Fishman, W. H., Green, S., and Inglis, N. I., L-Phenylalanine: An organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase, Nature (London), 198, 684, 1963.

    Google Scholar 

  341. Bernstine, E. G., Hooper, M. L., Grandchamp, S., and Ephrussi, B., Alkaline phosphatase in mouse teratoma, Proc. Natl. Acad. Sci. USA., 70, 3899, 1974.

    Google Scholar 

  342. Byers, D. A., Fernley, H. N., and Walker, P. G., Studies on alkaline phosphatase: Inhibition of human placental phosphoryl phosphatase by L-phenylalanine, Eur. J. Biochem., 29, 197, 1972.

    CAS  Google Scholar 

  343. Bodansky, O., The inhibitory effects of DL-alanine, L-glutamic acid, L-lysine and L-histidine on the activity of intestinal, bone and kidney phosphatases, J. Biol. Chem., 174, 465, 1948.

    CAS  Google Scholar 

  344. Bodansky, O., Influence of magnesium and cobalt on the inhibition of phosphatases of bone, intestine and osteogenic sarcoma by amino acids, J. Biol. Chem., 179, 81, 1949.

    CAS  Google Scholar 

  345. Zittle, C. A., and Della Monica, E. S., Effects of glutamic acid, lysine and certain inorganic ions on bovine alkaline phosphatases, Arch. Biochem., 26, 135, 1950.

    CAS  Google Scholar 

  346. Lustig, V., and Kellen, J. A., Species, organ and subcellular specificity of alkaline phosphtases as determined by amino acid inhibition studies, Comp. Biochem. Physiol., 39B, 305, 1971.

    CAS  Google Scholar 

  347. Lin, C. W., and Fishman, W. H., L-Homoarginine: An organ-specific uncompetitive inhibitor of human liver and bone alkaline phosphohydrolases, J. Biol. Chem., 247, 3082, 1972.

    CAS  Google Scholar 

  348. Fishman, W. H., and Sie, H. G., L-Homoarginine: An inhibitor of “bone and liver” alkaline phosphatase, Clin. Chim. Acta, 29, 339, 1970.

    CAS  Google Scholar 

  349. Lin, C. W., Sie, H. G., and Fishman, W. H., L-Tryptophan: A non-allosteric organ-specific uncompetitive inhibitor of human placental alkaline phosphatase, Biochem. J., 124, 509, 1971.

    CAS  Google Scholar 

  350. Jenner, H. D., and Kay, H. D., The phosphatases of mammalian tissues. III. Magnesium and the phosphatase system, J. Biol. Chem., Pi, 733, 1931.

    Google Scholar 

  351. Clark, B., and Porteous, J. W., The metal ion activation of the alkaline beta-glycerophosphatase of rabbit small intestine, Biochem. J., 95, 475, 1965.

    CAS  Google Scholar 

  352. Cloetens, R., Über den Aktivierungsmechanismus der alkalischen Phosphatase II durch Metallionen, Biochem. Z. 307, 352, 1941.

    CAS  Google Scholar 

  353. Fernley, H. N., Mammalian alkaline phosphatases, in: The Enzymes, Vol. 4 (Boyer, P. D., ed.), p. 417, Academic Press, New York, 1971.

    Google Scholar 

  354. Brunel, C., and Cathala, G., Activation and inhibition processes of alkaline phosphatases from bovine brain by metal ions (Mg2+ and Zn2+), Biochim. Biophys. Acta, 309, 104, 1973.

    CAS  Google Scholar 

  355. Cathala, G., and Brunel, C., L’activité pyrophosphatasique de la phosphatase alcaline du cerveau, Biochim. Biophys. Acta, 315, 73, 1973.

    CAS  Google Scholar 

  356. DuBois, K. P., Cochran, K. W., and Mazur, M., Inhibition of phosphatases by beryllium and antagonism of the inhibition by manganese, Science, 110, 420, 1949.

    Google Scholar 

  357. Schubert, J., and Lindenbaum, A., Studies on the mechanism of protection of aurin-tricarboxylic acid in beryllium poisoning. II. Equilibria involving alkaline phosphatase, J. Biol. Chem., 208, 359, 1954.

    CAS  Google Scholar 

  358. Thomas, M., and Aldridge, W. N., The inhibition of enzymes by beryllium, Biochem. J., 98, 94, 1966.

    CAS  Google Scholar 

  359. Tait, G. H., and Vallee, B. L., Studies on the active center of alkaline phosphatase of E. coli., Proc. Natl. Acad. Sci. U.S.A., 56, 1247, 1966.

    Google Scholar 

  360. Lazdunski, C., Petitclerc, C., Chappelet, D., Leterrier, F., Douzou, P., and Lazdunski, M., Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli,Biochem. Biophys. Res. Commun., 40, 589, 1970.

    CAS  Google Scholar 

  361. Nagode, L. A., Haussler, M. R., Boyce, D. W., Pechet, M., and Rasmussen, H., Vitamin-D induced phosphatases in bone and intestine: Inhibitions by theophylline and diphosphonates, Fed. Proc. Fed. Am. Soc. Exp. Biol., 29, 368, 1970.

    Google Scholar 

  362. Fawaz, N., and Tejirian, A., Inhibition of alkaline phosphatase by theophylline in vitro, Z. Physiol. Chem., 353, 1779, 1972.

    CAS  Google Scholar 

  363. Santachiara-Benerecetti, S. A., Cesari, I., and De Carli, L., Some properties of alkaline phosphatase from a human cell strain and from a clonal derivative with low activity, J. Cell. Physiol., 69, 169, 1967.

    CAS  Google Scholar 

  364. Glew, R. H., and Heath, E. C., Studies on the extracellular alkaline phosphatase of Micrococcus sodonensis. 1. Isolation and characterization, J. Biol. Chem., 246, 1556, 1971.

    CAS  Google Scholar 

  365. Saini, P. K., and Posen, S., The origin of serum alkaline phosphatase in the rat, Biochim. Biophys. Acta, 7 77, 42, 1969.

    Google Scholar 

  366. Freeman, S., and Chen, Y. P., The effect of jaundiced blood upon normal dogs with special reference to the serum phosphatase, J. Biol. Chem., 123, 239, 1938.

    CAS  Google Scholar 

  367. Cantarow, A., and Miller, L. L., Nonexcretion of jaundice-serum alkaline phosphatase in bile of normal dogs, Am. J. Physiol., 153, 444, 1948.

    CAS  Google Scholar 

  368. Dalgaard, J. B., Serum phosphatase after transfusion of phosphatase-rich blood to normal dogs, Acta Physiol. Scand., 22, 193, 1951.

    CAS  Google Scholar 

  369. Crystle, C. D., Breuning, F., Dubin, N. H., Grannis, G. F., Stevens, V. C., and Townley, J. D., Blood disappearance rates of certain hormones and enzymes advocated as fetoplacental function tests, Obstet. Gynecol., 43, 41, 1974.

    CAS  Google Scholar 

  370. Posen, S., Turnover of circulating enzymes, Clin. Chem., 16, 11, 1970.

    Google Scholar 

  371. Reynoso, G., Elias, E. G., and Mittelman, A., The contribution of the intestinal mucosa to the total serum alkaline phosphatase activity, Am. J. Clin. Pathol., 56, 707, 1971.

    CAS  Google Scholar 

  372. Chen, Y. P., Freeman, S., and Ivy, A. C., The preparation of a concentrated fecal phosphatase and its effect on dogs and rats, J. Biol. Chem., 132, 445, 1940.

    Google Scholar 

  373. Stolbach, L., Skillman, J., and Goodman, R., Increase in serum alkaline phosphatase due to Regan isoenzyme in a patient with localized jejunal lymphoma, Arch. Surg., 105, 491, 1972.

    CAS  Google Scholar 

  374. Bodon, G. R., and Mijangos, J. A., Alkaline phosphatase-producing leiomyosarcoma of the uterus, Am. J. Surg., 124, 673, 1972.

    CAS  Google Scholar 

  375. Massarrat, S., and Massarrat, S., Origin of serum alkaline phosphatase in hepatobiliary diseases, Enzyme, 72, 593, 1971.

    Google Scholar 

  376. Armstrong, A. R., King, E. J., and Harris, I., Phosphatase in obstructive jaundice, Can. Med. Assoc. J., 31, 14, 1934.

    CAS  Google Scholar 

  377. Carr, J. L., and Foote, F. S., Alkaline and acid phosphatase levels in the serum of dogs after ligation of the common bile duct, Arch. Surg., 49, 44, 1944.

    CAS  Google Scholar 

  378. Rothman, F., and Byrne, R., Fingerprint analysis of alkaline phosphatase of Escherichia coli K12, J.Mol. Biol., 6, 330, 1963.

    CAS  Google Scholar 

  379. Gottlieb, A. J., and Sussman, H. H., Human placental alkaline phosphatase: Molecular weight and subunit structure, Biochim. Biophys. Acta, 160, 167, 1968.

    CAS  Google Scholar 

  380. Thomas, L., and Kinne, R., Studies on the arrangement of aminopeptidase and alkaline phosphatase in the microvilli of isolated brush border of rat kidney, Biochim. Biophys. Acta, 255, 114, 1972.

    CAS  Google Scholar 

  381. Sussman, H. H., and Gottlieb, A. J., Human placental alkaline phosphatase. II. Molecular and subunit properties of the enzyme, Biochim. Biophys. Acta, 194, 170, 1969.

    CAS  Google Scholar 

  382. Simpson, R. T., Vallee, B. L., and Tait, G. H., Alkaline phosphatase of Escherichia coli: Composition, Biochemistry, 7, 4336, 1965.

    Google Scholar 

  383. Csopak, H., Garellick, G., and Hallberg, B., Purification of Escherichia coli alkaline phosphatase: Improved growth conditions for the bacteria, modified methods of preparation of the enzyme, Acta Chem. Scand., 26, 2401, 1972.

    CAS  Google Scholar 

  384. Day, D. F., and Ingram, J. M., Purification and characterization of Pseudomonas aeruginosa alkaline phosphatase, Can. J.Microbiol., 19, 1225, 1973.

    CAS  Google Scholar 

  385. Schwartz, J. H., Crestfield, A. M., and Lipmann, F., The amino acid sequence of a tetradecapeptide containing the reactive serine in E. coli alkaline phosphatase, Proc. Natl. Acad. Sci. U.S.A., 49, 722, 1963.

    CAS  Google Scholar 

  386. Zwaig, N., and Milstein, C., The amino-acid sequence around the reactive serine residue in alkaline phosphatase of Serratia marcescens, Biochem. J., 92, 421, 1964.

    CAS  Google Scholar 

  387. Schlesinger, S., and Schlesinger, M. J., The effect of amino acid analogues on alkaline phosphatase formation in Escherichia coli Kl2. III. Substitution of 2 methylhistidine for histidine, J. Biol. Chem., 244. 3803, 1969.

    CAS  Google Scholar 

  388. Schlesinger, S., The effect of amino acid analogues on alkaline phosphatase formation in Escherichia coli Kl2. II. Replacement of tryptophan by azatryptophan and tryptazan, J. Biol. Chem., 243, 3877, 1968.

    CAS  Google Scholar 

  389. Attias, J., Schlesinger, M. J., and Schlesinger, S., The effect of amino acid analogues on alkaline phosphatase formation in Escherichia coli K-12. IV. Substitution of canavanine for arginine, J. Biol. Chem., 244, 3810, 1969.

    CAS  Google Scholar 

  390. Malamy, M. H., and Horecker, B. H., Crystallisation of E. coli alkaline phosphatase, Biochemistry, 3, 1893, 1964.

    CAS  Google Scholar 

  391. Kadner, R. J., Nyc, J. F., and Brown, D. M., A repressible alkaline phosphatase in Neurospora crassa, J. Biol. Chem., 243, 3076, 1968.

    CAS  Google Scholar 

  392. Ghosh, N. K., Goldman, S. S., and Fishman, W. H., Human placental alkaline phosphatases: A sialoprotein, Enzymologia, 33, 113, 1967.

    CAS  Google Scholar 

  393. Butterworth, P. J., and Moss, D. W., Action of neuraminidase on human kidney alkaline phosphatase, Nature (London), 209, 805, 1966.

    CAS  Google Scholar 

  394. Moss, D. W., Eaton, R. H., Smith, J. K., and Whitby, L. G., Alteration in the electrophoretic mobility of alkaline phosphatases after treatment with neuraminidase, Biochem. J., 98, 32c, 1966.

    Google Scholar 

  395. Chang, C. H., and Moog, F., Alkaline phosphatases of the chicken duodenum. II. Enzyme dissociation of a large phosphatase complex predominant in the duodenum before hatching, Biochim. Biophys. Acta, 258, 166, 1972.

    CAS  Google Scholar 

  396. Reynolds, J. A., and Schlesinger, M. S., Conformational states of the subunit of Escherichia coli alkaline phosphatase, Biochemistry, 6, 3552, 1967.

    CAS  Google Scholar 

  397. Reynolds, J. A., and Schlesinger, M. J., Hydrogen ion equilibria of conformational states of Escherichia coli alkaline phosphatase, Biochemistry, 7, 2080, 1968.

    CAS  Google Scholar 

  398. Halford, S. E., Lennette, D. A., Kelley, P. M., and Schlesinger, M. J., A mutationally altered alkaline phosphatase from Escherichia coli. 1. Formation of an active enzyme in vitro and phenotypic suppression in vivo, J. Biol. Chem., 247, 2087, 1972.

    CAS  Google Scholar 

  399. Vallee, B. L., and Williams, R. J. P., Metalloenzymes: The entatic nature of their active sites, Proc. Natl. Acad. Sci. U.S.A., 59, 498, 1968.

    CAS  Google Scholar 

  400. Prasad, A. S., Oberleas, D., Wolf, P., Horwitz, J. P., Miller, E. R., and Luecke, R. W., Changes in trace elements and enzyme activities in tissues of zinc deficient pigs, Am. J. Clin.Nutr., 22, 628, 1969.

    CAS  Google Scholar 

  401. Reinhold, J. G., and Kfoury, G. A., Zinc-dependent enzymes in zinc-depleted rats; Intestinal alkaline phosphatase, Am. J. Clin.Nutr. 22, 1250, 1969.

    CAS  Google Scholar 

  402. Shrader, R. E., and Hurley, L. S., Enzyme histochemistry of peripheral blood and bone marrow in zinc-deficient rats, Lab. Invest., 26, 566, 1972.

    CAS  Google Scholar 

  403. Knox, J. R., and Wyckoff, H. W., A crystallographic study of alkaline phosphatase at 7.7 A resolution, J. Mol. Biol., 74, 5 3 3, 1973.

    Google Scholar 

  404. Applebury, M. L., and Coleman, J. E., Escherichia coli alkaline phosphatase: Metal binding protein conformation, and quarternary structure, J. Biol. Chem., 244, 308, 1969.

    CAS  Google Scholar 

  405. Horne, M., Cornish, C. J., and Posen, S., The use of urea denaturation in the identification of human alkaline phosphatases, J. Lab. Clin. Med., 72, 905, 1968.

    CAS  Google Scholar 

  406. Beckman, L., Bjorling, G., and Christodoulou, C., Pregnancy enzymes and placental polymorphism. 1. Alkaline phosphatase, Acta Genet. (Basel), 16, 59, 1966.

    CAS  Google Scholar 

  407. Blake, N. M., Kirk, R. L., and Osathanondh, V., Placental alkaline phosphatase types in Thailand, Med. J. Aust., 2, 1042, 1968.

    CAS  Google Scholar 

  408. Ishimoto, G., Distribution of placental alkaline phosphatase types in a Japanese population, Hum. Hered., 20, 193, 1970.

    CAS  Google Scholar 

  409. Johnson, F. M., Drosophila melanogaster: Inheritance of a deficiency of alkaline phosphatase in larvae, Science, 152, 361, 1966.

    CAS  Google Scholar 

  410. Beckman, G., Placental alkaline phosphatase, relation between phenotype and enzyme activity, Hum. Hered., 20, 74, 1970.

    CAS  Google Scholar 

  411. Beratis, N. G., Seegers, W., and Hirschhorn, K., Properties of placental alkaline phosphatase. II. Interactions of fast- and slow-migrating components, Biochem. Genet., 5, 367, 1971.

    CAS  Google Scholar 

  412. Edwards, J. H., and Wingham, J., Data on linkage between the locus determining placental alkaline phosphatase (P1) and other markers, Ann. Hum. Genet. (London), 30, 233, 1967.

    CAS  Google Scholar 

  413. Bottini, E., Lucarelli, P., and Gloria, F., Placental alkaline phosphatase and ABO system polymorphisms: Analysis of relationships among gene frequencies in human populations. Further evidence at the population level for an interaction between the two polymorphisms, Am. J. Hum. Genet., 24, 505, 1972.

    CAS  Google Scholar 

  414. Beckman, G., Beckman, L., and Magnusson, S. S., Placental alkaline phosphatase phenotypes and pre-natal selection: Evidence from spontaneous and induced abortions, Hum. Hered., 22, 473, 1972.

    CAS  Google Scholar 

  415. Bottini, E., Lucarelli, P., Pigram, P., Palmarino, R., Spennati, G. F., and Orzatesi, M., Interaction between placental alkaline phosphatase and ABO system polymorphisms during intrauterine life, Am. J. Hum. Genet., 24, 495, 1972.

    CAS  Google Scholar 

  416. Watson, D., Weston, W., and Porter, R., Plasma alkaline phosphatases in normal and abnormal terminal pregnancy, Enzymol. Biol. Clin., 5, 25, 1965.

    CAS  Google Scholar 

  417. Neri, A., and Korngold, L., Immunologic properties of alkaline phosphatase from human placenta and membrane at delivery, Am. J. Obstet. Gynecol., 107, 1047, 1970.

    CAS  Google Scholar 

  418. Beckman, L., and Regan, J. D., Isozyme studies of some human cell lines, Acta Pathol. Microbiol. Scand., 62, 561, 1964.

    Google Scholar 

  419. Sherman, M. I., The biochemistry of differentiation of mouse trophoblast alkaline phosphatase, Dev. Biol., 27, 337, 1972.

    CAS  Google Scholar 

  420. Gomori, G., The complex nature of alkaline phosphatase, Biochim. Biophys. Acta, 8, 162, 1952.

    CAS  Google Scholar 

  421. Behal, F. J., and Center, M., Heterogeneity of calf intestinal alkaline phosphatase, Arch. Biochem. Biophys., 110, 500, 1965.

    Google Scholar 

  422. Moog, F., and Yeh, K. Y., Intestinal alkaline phosphatase of the rat: Development of distribution of activity with phenylphosphate and beta-glycerophosphate, Comp. Biochem. Physiol., 44B, 651, 1973.

    Google Scholar 

  423. Lafont, J., and Roziere, J., Heterogeneity dependent on age intestinal alkaline phosphatase in the rat, Comp. Biochem. Physiol., 45B, 135, 1973.

    CAS  Google Scholar 

  424. Fabricius-Bjerre, N., Hanel, H. K., and Holst-Christensen, J., Alkaline phosphatase in colorectal cancer: A quantitative analysis of the enzyme content, Scand. J. Gastroenterol., 7, 369, 1972.

    CAS  Google Scholar 

  425. Saini, P. K., Studies of alkaline phosphatase in membranes of rat tissues, Ph.D. thesis, University of Sydney, 1970.

    Google Scholar 

  426. Moog, F., Intestinal phosphatase activity: Acceleration of increase by puromycin and actinomycin, Science, 144, 414, 1964.

    CAS  Google Scholar 

  427. Moog, F., and Grey, R., Spatial and temporal differentiation of alkaline phosphatase on the intestinal villi of the mouse, J. Cell Biol.,32, CI, 1967.

    Google Scholar 

  428. Nordstrom, C., Dahlqvist, A., and Josefsson, L., Quantitative determination of enzymes in different parts of the villi and crypts of rat small intestine: Comparison of alkaline phosphatase, disaccharidases and dipeptidases, J. Histochem. Cytochem., 15, 713, 1967.

    CAS  Google Scholar 

  429. Nordstrom, C., and Dahlqvist, A., Quantitative distribution of some enzymes along the villi and crypts of human small intestine, Scand. J. Gastroentrol., 8, 407, 1973.

    Google Scholar 

  430. Moog, F., The functional differentiation of the small intestine. I. The accumulation of alkaline phosphatase in the duodenum of the chick, J. Exp. Zool., 115, 109, 1950.

    CAS  Google Scholar 

  431. Moog, F., The functional differentiation of the small intestine. II. The differentiation of alkaline phosphomonoesterase in the duodenum of the mouse, J. Exp. Zool., 118, 187, 1951.

    Google Scholar 

  432. Moog, F., and Ortiz, E., The functional differentiation of the small intestine. VII. The duodenum of the foetal guinea-pig with a note on the growth of the adrenals, J. Embryol. Exp. Morphol., 8, 182, 1960.

    CAS  Google Scholar 

  433. Moog, F., The regulation of alkaline phosphatase activity in the duodenum of the mouse from birth to maturity, J. Exp. Zool., 161, 353, 1966.

    CAS  Google Scholar 

  434. Moog, F., The functional differentiation of the small intestine. III. The influence of the pituitary adrenal system on the differentiation of phosphatase in the duodenum of the suckling mouse, J. Exp. Zool., 124, 329, 1953.

    CAS  Google Scholar 

  435. Halliday, R., The increase in alkaline phosphatase of the duodenum and decrease in absorption of antibodies by the gut induced in young rats by deoxycorticosterone acetate, J. Physiol (London), 140, 44, 1958.

    CAS  Google Scholar 

  436. Halliday, R., The effect of steroid hormones on the absorption of antibody by the young rat, J. Endocrinol, 18, 56, 1959.

    CAS  Google Scholar 

  437. Pataryas, H. A., and Christodoulou, C., Alterations in human organ alkaline phosphatases during foetal development, Hum. Hered., 20, 420, 1970.

    CAS  Google Scholar 

  438. Hernandez-Jodra, M., and Gancedo, C., Isoenzymes of alkaline phosphatase in human meconium and small intestine during development, Enzyme, 12, 682, 1971.

    CAS  Google Scholar 

  439. Madsen, N. B., and Tuba, J., On the source of the alkaline phosphatase in rat serum, J. Biol Chem., 195, 741, 1952.

    CAS  Google Scholar 

  440. Nayudu, P. R. V., and Moog, F., Intestinal alkaline phosphatase: Regulation by a strain-specific tactor in mouse milk, Science, 152, 656, 1966.

    CAS  Google Scholar 

  441. Savage, D. C., Association and physiological interactions of indigenous microorganisms and gastrointestinal epithelia, Am. J. Clin. Nutr., 25, 1372, 1972.

    Google Scholar 

  442. Whitmore, D., and Goldberg, E., Molecular heterogenitity of alkaline phosphatase in trout, Physiol Chem. Phys., 1, 339, 1969.

    CAS  Google Scholar 

  443. Schussler, H., Über die chromatographisohe Auftrennung sowie Aktivierung und Inaktivierung der alkalischen Phosphatase aus Hühnerdarm,Biochim. Biophys. Acta, 151, 383, 1968.

    CAS  Google Scholar 

  444. Weiser, M. M., Bolt, R. J., and Pollard, H. M., Isozyme patterns of the human gastrointestinal tract in the normal state and in nontropical sprue, J. Lab. Clin. Med., 63, 656, 1964.

    CAS  Google Scholar 

  445. Lumb, J. R., and Doell, R. G., The biochemical characterization of alkaline phosphatase from chemical- and viral-induced thymic lymphomas of C57 BL mice, Cancer Res., 30, 1391, 1970.

    CAS  Google Scholar 

  446. Herz, F., and Nitowsky, H. M., Alkaline phosphatase activity of human cell cultures: Kinetic and physical chemical properties, Arch. Biochem. Biophys, 96, 306, 1962.

    Google Scholar 

  447. Marcus, D. M., The ABO and Lewis blood group system: Immunochemistry, genetics and relation to human disease, N. Engl. J. Med., 280, 994, 1969.

    CAS  Google Scholar 

  448. Gahne, B., Inherited high alkaline phosphatase activity in cattle serum, Hereditas, 57, 83, 1967.

    CAS  Google Scholar 

  449. Poulik, M. D., Starch-gel electrophoresis in a discontinuous system of buffers, Nature (London), 180, 1477, 1957.

    CAS  Google Scholar 

  450. Woodard, H. Q., Quantitative studies of beta glycerophosphatase in normal and neoplastic tissues, Cancer, 9, 352, 1956.

    CAS  Google Scholar 

  451. Jeffree, G. M., Phosphatase activity in the limb bones of monkeys (Lagothrix humboldti) with hyperparathyroidism, J. Clin. Pathol., 15, 99, 1962.

    CAS  Google Scholar 

  452. Jeffree, G. M., and Price, C. H. G., Bone tumours and their enzymes: A study of the phosphatases, non-specific esterases and beta glucuronidase of osteogenic and cartilaginous tumours, fibroblastic and giant-cell lesions, J. Bone Joint Surg., 47B, 120, 1965.

    CAS  Google Scholar 

  453. Makinen, K. K., and Paunio, I. K., Evidence on certain common properties of alkaline phosphatase-like enzymes derived from human foetal mineralizing tissues, FEBS Lett., 3, 153, 1969.

    Google Scholar 

  454. Makinen, K. K., and Knuuttila, M. L., Concerning the similarities between three alkaline phosphatases of human foetal parietal bones, Calcif. Tissue Res., 9, 28, 1972.

    CAS  Google Scholar 

  455. Linde, A. and Magnusson, B. C., Inhibition studies of alkaline phosphatases in hard tissue- forming cells, J. Histochem. Cytochem., 23, 342, 1975.

    CAS  Google Scholar 

  456. Reynolds, J. J., and Dew, G. W., Comparison of the inhibition of avian and mammalian bone alkaline phosphatases by levamisole and compount R8231, Experientia, 33, 154, 1977.

    CAS  Google Scholar 

  457. Ozsoylu, S., Leukocyte alkaline phosphatase activity in rickets due to Vitamin D deficiency, N. Engl J. Med., 280, 1221, 1969.

    CAS  Google Scholar 

  458. Browne, M. S., Pitts, M. W., and Pitts, R. F., Alkaline phosphatase activity in kidneys of glomerular and aglomerular marine teleosts, Biol Bull., 99, 152, 1950.

    CAS  Google Scholar 

  459. George, S. G., and Kenny, A. J., Studies on the enzymology of purified preparations of brush border from rabbit kidney, Biochem. J., 134, 43, 1973.

    CAS  Google Scholar 

  460. Viek, N. F., Uhlman, R. C., and Verrilli, R. A., Studies of alkaline phosphatase in various pathological conditions of the kidney. 1. Renal injury, J. Urol., 85, 714, 1961.

    CAS  Google Scholar 

  461. Dalgaard, J. B., Serum phosphatase after nephrectomy and bile obstruction in dogs., Acta Physiol Scand., 16, 318, 1949.

    CAS  Google Scholar 

  462. Grunstein, H. S., Yriberri, J., and Posen, S., Calcitonin’s role, N. Engl J. Med., 297, 401, 1977.

    Google Scholar 

  463. Schales, O., and Arai, K., Preparation and properties of highly purified alkaline kidney phosphatase, Arch. Biochem. Biophys., 83, 152, 1959.

    CAS  Google Scholar 

  464. Finegan, R. P., Multiple nature of alkaline phosphatase in the mammalian kidney, Nature (London), 198, 193, 1963.

    Google Scholar 

  465. Rhone, D. P., and Mizuno, F. M., Separation of isoenzymes of alkaline phosphatase by substrate-gel imprint after electrophoresis on cellulose acetate, Clin. Chem., 18, 662, 1972.

    CAS  Google Scholar 

  466. Pope, C. E., and Cooperband, S. R., Protein characteristics of serum and bile alkaline phosphatase, Gastroenterology, 50, 631, 1966.

    CAS  Google Scholar 

  467. Lorentz, K., Niemann, E., Jaspers, G., and Oltmanns, D., Enzyme in der menschlichen Galle, Enzymol. Biol Clin., 10, 528, 1969.

    CAS  Google Scholar 

  468. Posen, S., Alkaline phosphatase, Ann. Intern. Med., 67, 183, 1967.

    CAS  Google Scholar 

  469. Bode, J. C., Zelder, O., and Neuberger, H. O., Effect of taurocholate, dehydrocholate and secretin on biliary output of alkaline phosphatase and GOT,Helv. Med. Acta, 37, 143, 1973.

    CAS  Google Scholar 

  470. Dyck, W. P., Martin, G. A., and Ratliff, C. R., Influence of secretin and cholecystokinin on intestinal alkaline phosphatase activity, Gastroenterology, 64, 599, 1973.

    CAS  Google Scholar 

  471. Sussman, H. H., Small, P. A., and Cotlove, E., Human alkaline phosphatase: Immunochemical identification of organ-specific isoenzymes, J. Biol Chem., 243, 160, 1968.

    CAS  Google Scholar 

  472. Nitowsky, H. M., and Herz, F., Alkaline phosphatase in cell cultures of human origin, Nature (London), 189, 756, 1961.

    CAS  Google Scholar 

  473. Armstrong, A. R., and Banting, F. G., The site of formation of the phosphatase of serum, Can. Med. Assoc. J., 33, 243, 1935.

    CAS  Google Scholar 

  474. Gould, B. S., Studies on the source of serum phosphatase: The nature of the increased serum phosphatase in rats after fat feeding, Arch. Biochem., 4, 175, 1944.

    CAS  Google Scholar 

  475. Stafford, R. O., and Atkinson, W. B., Effect of acetone and alcohol fixation and paraffin embedding on activity of acid and alkaline phosphatases in rat tissues, Science, 107, 279, 1948.

    CAS  Google Scholar 

  476. Warnock, M. L., and Reisman, R., Variant alkaline phosphatase in human hepatocellular cancers, Clin. Chim. Acta, 24, 5, 1969.

    CAS  Google Scholar 

  477. Pekarthy, J. M., Short, J., Lansing, A. I., and Lieberman, I., Function and control of liver alkaline phosphatase, J. Biol Chem., 247, 1767, 1972.

    CAS  Google Scholar 

  478. Baker, A., Kaplan, M., and Kimberg, D. V., Alkaline phosphatase: Possible induction by cyclic AMP after cholera enterotoxin administration, J. Clin. Invest., 52, 2928, 1973.

    CAS  Google Scholar 

  479. Moss, D. W., Panov, E. Y., and Whitaker, K. B., The effect of biliary obstruction on some properties of alkaline phosphatase of rat liver, Clin. Chim. Acta, 51, 41, 1974.

    CAS  Google Scholar 

  480. Cory, J. G., Whitford, T. W., and Rich, M. A., Alkaline phosphatase activity in virus-induced murine leukemia, Biochem. Med., 5, 465, 1971.

    CAS  Google Scholar 

  481. Righetti, A. B. B., Kaplan, M. M., and Raben, M. S., Properties of rat liver alkaline phosphatase before and after bile duct ligation, Proc. Soc. Exp. Biol Med., 145, 726, 1974.

    CAS  Google Scholar 

  482. Hall, K., Lactic dehydrogenase and other enzymes in the mouse uterus during the peri-implantation period of pregnancy,J. Reprod. Fertil., 34, 79, 1973.

    Google Scholar 

  483. Manning, J. P., Steinetz, B. G., and Giannina, T., Decidual alkaline phosphatase activity in the pregnant and pseudo-pregnant rat, Ann. N. Y. Acad. Sci., 166, 482, 1969.

    CAS  Google Scholar 

  484. Baba, N., Vidyarthi, S., and Von Haam, E., Nonspecific phosphatases of rabbit endometrial carcinoma, Arch. Pathol, 90, 65, 1970.

    CAS  Google Scholar 

  485. Murdoch, R. N., Some biochemical and kinetic properties of sheep uterine endometrial alkaline phosphatase, Aust. J. Biol Sci., 24, 331, 1971.

    CAS  Google Scholar 

  486. Dufour, D., Tremblay, A., Taskar, S., and Estrada, R., Organ and species specificity of mouse uterine alkaline phosphatase, J. Exp. Zool., 179, 263, 1972.

    CAS  Google Scholar 

  487. Wilson, E. W., Personal communication, 1974.

    Google Scholar 

  488. Wilson, E. W., The effect of metallic copper on human endometrial alkaline phosphatase activity, J. Obstet. Gynaecol Br. Commonw., 80, 648, 1973.

    CAS  Google Scholar 

  489. Gey, G. W., Coffman, W. D., and Kubicek, M. T., Tissue culture studies of the proliferative capacity of cervical carcinoma and normal epithelium, Cancer Res., 12, 264, 1952.

    Google Scholar 

  490. Scherer, W. F., Syverton, J. T., and Gey, G. O., Studies on the propagation in vitro of polio¬myelitis viruses. IV. Viral multiplication in a stable strain of human malignant epithelial cells (strain HeLa) derived from an epidermoid carcinoma of the cervix, J. Exp. Med., 97, 695, 1953.

    CAS  Google Scholar 

  491. Cox, R. P., and MacLeod, C. M., Hormonal induction of alkaline phosphatase in human cells in tissue culture, Nature (London), 190, 85, 1961.

    CAS  Google Scholar 

  492. Elson, N. A., and Cox, R. P., Production of fetal-like alkaline phosphatase by HeLa cells, Biochem. Genet., 3, 549, 1969.

    CAS  Google Scholar 

  493. Cox, R. P., and MacLeod, C. M., Regulation of alkaline phosphatase in human cell cultures, Cold Spring Harbor Symp. Quant. Biol., 29, 233, 1964.

    CAS  Google Scholar 

  494. Melnykovych, G., and Bishop, C. F., Specificity of prednisolone effect on cell volume, RNA and protein in cell lines with inducible and noninducible alkaline phosphatase, Endocrinology, 81, 251, 1967.

    CAS  Google Scholar 

  495. Melnykovych, G., and Costlow, C. C., Relationship between glucosamine uptake and alkaline phosphatase in HeLa cells: Effects of glucose and prednisolone, J. Natl. Cancer Inst., 47, 521, 1971.

    Google Scholar 

  496. Herz, F., and Sevdalian, D. A., Regulation of alkaline phosphatase activity in human cell cultures: Role of serum, Arch. Biochem. Biophys., 146, 1, 1971.

    CAS  Google Scholar 

  497. Griffin, M. J., and Bottomley, R. H., Regulation of alkaline phosphatase in HeLa clones of differing modal chromosome number, Ann. N. Y. Acad. Sci., 166, All, 1969.

    Google Scholar 

  498. Spencer, T., Action of Sendai virus and neuraminidase on the alkaline phosphatase isoenzymes of HeLa cells, Nature (London), 215, 985, 1967.

    CAS  Google Scholar 

  499. Spencer, T., Some factors controlling alkaline phosphatase isoenzymes in HeLa cells, Biochem. J., 116, 921, 1970.

    Google Scholar 

  500. Ghosh, N. K., Rukenstein, A., Baltimore, R., and Cox, R. P., Studies on hormonal induction of alkaline phosphatase in HeLa cell cultures, kinetic, thermodynamic and electrophoretic properties of induced and base level enzymes, Biochim. Biophys. Acta, 286, 175, 1972.

    CAS  Google Scholar 

  501. Fishman, W. H., Inglis, N. I., Stolbach, L. L., and Krant, M. J., A serum alkaline phosphatase isoenzyme of human neoplastic cell origin, Cancer Res., 28, 150, 1968.

    CAS  Google Scholar 

  502. Tan, K. K., and Aw, S. E., Immunological studies on HeLa cell heat-stable alkaline phosphatases and their antigenic relationship with human placental and intestinal iso-enzymes,Immunochemistry, 10, 209, 1973.

    CAS  Google Scholar 

  503. Wachstein, M., Alkaline phosphatase activity in normal and abnormal human blood and bone marrow cells, J. Lab. Clin. Med., 31, 1, 1946.

    CAS  Google Scholar 

  504. Moloney, W. C., Leukocyte alkaline phosphatase activity in the rat, Ann. N. Y. Acad. Sci., 75, 31, 1958.

    CAS  Google Scholar 

  505. Rosner, F., and Lee, S. L., Zinc and magnesium content of leukocyte alkaline phosphatase isoenzymes, J. Lab. Clin. Med., 79, 228, 1972.

    CAS  Google Scholar 

  506. Valentine, W. N., and Beck, W. S., Biochemical studies on leucocytes. I. Phosphatase activity in health, leucocytosis and myelocytic leucemia,J. Lab. Clin. Med., 38, 39, 1951.

    CAS  Google Scholar 

  507. Avila, J. L., and Convit, J., Studies on human polymorphonuclear leukocyte enzymes. 1. Assay of acid hydrolases and other enzymes, Biochim. Biophys. Acta, 293, 397, 1973.

    CAS  Google Scholar 

  508. Stein, I. D., and Rubini, J. R., Thymidylate dephosphorylation in granulocytes, Proc. Soc. Exp. Biol Med., 120, 314, 1965.

    Google Scholar 

  509. Monteleone, P. L., Nadler, H. L., Pi, C. S., and Hsia, D. Y. Y., Isoenzymes in Down’s syndrome, Lancet, 2, 367, 1967.

    Google Scholar 

  510. King, M. J., Gillis, E. M., and Baikie, A. G., Alkaline phosphatase activity of polymorphs in mongolism, Lancet, 2, 1302, 1962.

    CAS  Google Scholar 

  511. Alter, A. A., Lee, S. L., Pourfar, M., and Dobkin, G., Studies of leukocyte alkaline phosphatase in mongolism: A possible chromosome marker, Blood, 22, 165, 1963.

    CAS  Google Scholar 

  512. Phillips, J., Herring, R. M., Goodman, H. O., and King, J. S., Leukocyte alkaline phosphatase and erythrocyte glucose-6-phosphate dehydrogenase in Down’s syndrome, J. Med. Genet., 4, 268, 1967.

    CAS  Google Scholar 

  513. Robinson, J. C., Pierce, J. E., and Goldstein, D. P., Leukocyte alkaline phosphatase: Electrophoretic variants associated with chronic myelogenous leukemia, Science, 150, 58, 1965.

    CAS  Google Scholar 

  514. Robinson, J. C., Pierce, J. E., Goldstein, D. P., and Rosse, W. R., Leukocyte-alkaline-phosphatase isozymes, Lancet, 2, 805, 1966.

    Google Scholar 

  515. Trubowitz, S., and Miller, W. L., Electrophoretic heterogeneity of leukocyte alkaline phosphatase in normal man and in patients with polycythemia vera, Proc. Soc. Exp. Biol. Med., 123, 187, 1966.

    CAS  Google Scholar 

  516. Lyons, R. B., Weaver, D. D., and Beck, J. H., Isoenzymes of human leukocyte alkaline phosphatase, Ann. N. Y. Acad. Sci., 155, 948, 1968.

    CAS  Google Scholar 

  517. Weaver, D. D., and Lyons, R. B., Leukocyte alkaline phosphatase isoenzymes, Lancet, 1, 1196, 1968.

    CAS  Google Scholar 

  518. Klein, U. E., Isoenzyme der alkalischen Phosphatase: Klinische Bedeutung, Zytotopik und mögliche Funktion, Dtsch. Med. Wochenschr. 94, 526, 1969.

    CAS  Google Scholar 

  519. Bottomley, R. M., Lovig, C. A., Holt, R., and Griffin, M. J., Comparison of alkaline phosphatase from human normal and leukemic leukocytes, Cancer Res., 29, 1866, 1969.

    CAS  Google Scholar 

  520. Rosenblum, D., and Petzold, S. J., Granulocyte alkaline phosphatase: Studies of purified enzymes from normal subjects and patients with polycythemia vera, J. Gin. Invest., 52, 1665, 1973.

    CAS  Google Scholar 

  521. Henson, P. M., The immunologic release of constituents from neutrophil leukocytes. II. Mechanisms of release during phagocytosis and adherence to nonphagocytosable surfaces, J. Immunol., 107, 1547, 1971.

    CAS  Google Scholar 

  522. Cao, A., Coppa, G., Marcucci, F., and Furbetta, M., Alkaline phosphatase and lactate dehydrogenase isoenzymes of human eosinophils, Clin. Chim. Acta, 45, 101, 1973.

    CAS  Google Scholar 

  523. Tangheroni, W., Cao, A., Lungarotti, S., Coppa, G., De Virgiliis, S., and Furbetta, M., Characterization of platelet alkaline phosphatase in normal subjects and in trisomy 21 Down’s syndrome patients, Clin. Chim. Acta, 35, 165, 1971.

    CAS  Google Scholar 

  524. Rapoport, S., Leva, E., and Guest, G. M., Acid and alkaline phosphatase and nucleophosphatase in the erythrocytes of some lower vertebrates, J. Cell. Comp. Physiol., 19, 103, 1942.

    CAS  Google Scholar 

  525. Behrendt, H., Phosphatase activity of human erythrocytes, Proc. Soc. Exp. Biol. Med., 54, 268, 1943.

    CAS  Google Scholar 

  526. Behrendt, H., Phosphatases in blood of man: Values in whole blood, plasma, cytolysates and erythrocytic suspensions, Am. J. Gin. Pathol., 19, 167, 1949.

    CAS  Google Scholar 

  527. Loffler, H., and Pralle, H., Nachweis von alkalischer Phosphataseaktivität in Erythrocyten bei einer familiären Polyglobulie, Verh. Dtsch. Ges. Inn. Med., 76, 530, 1970.

    Google Scholar 

  528. Pralle, H., Schnellbacher, E., and Loffler, H., Alkaline phosphatase in human erythrocytes: A new hereditary disorder, in: Erythrocytes, Thrombocytes, Leukocytes: Recent Advances in Membrane and Metabolic Research, IInd International Symposium, p. 189, Geo. Thieme, Stutt¬gart, 1973.

    Google Scholar 

  529. Pralle, H., Schnellbacher, E., and Loffler, H., Anreicherung und Eigenschaften von alkalischer Phosphatase aus Erythrocyten bei familiären Erythrocytose, Clin. Chim. Acta, 46, 363, 1973.

    CAS  Google Scholar 

  530. Baetz, A. L., Acid phosphatase, alkaline phosphatase, aspartate aminotransferase, alanine aminotransferase, creatine Phosphokinase and ornithine carbamyl transferase levels in blood and various tissues of calf, sheep, swine, horse, goat, chicken and turkey as determined on the Auto-Analyzer, in: Advances in Automated Analysis, Vol. 3, p. 163, Mediad, White Plains, New York, 1970.

    Google Scholar 

  531. Fell, H., and Danielli, J. F., The enzymes of healing wounds. I. The distribution of alkaline Phosphomonoesterase in experimental wounds and burns in the rat, Brit. J. Exp. Pathol., 24, 196, 1943.

    CAS  Google Scholar 

  532. Fry, A. E., Leius, V. K., Bacher, B. E., and Kaltenbach, J. C., Histochemical patterns in the tadpole tail during normal and thyroxine-induced metamorphosis. 1. Alkaline phosphatase, acid phosphatase, esterase and aminopeptidase, Gen. Comp. Endocrinol. 21, 16, 1973.

    CAS  Google Scholar 

  533. Johnson, W. C., and Alkek, D. S., Histopathology and histochemistry of cutaneous calciphylaxis, Clin. Orthop. 69, 75, 1970.

    CAS  Google Scholar 

  534. Solomon, R. D., Nadkarni, B. B., and Richardson, L., Local calciphylaxis in dihydrotachysterolsensitised rats: The role of alkaline phosphatase, Arch. Pathol., 82, 60, 1966.

    CAS  Google Scholar 

  535. Kornguth, M. L., and Stubbs, E. A. Hydrolysis of phosphohydroxypyruvate and beta-glycerophosphate by a phosphatase preparation from beef brain. Arch. Biochem. Biophys., 109, 104, 1965.

    CAS  Google Scholar 

  536. Saraswathi, S., and Bachhawat, B. K., Role of neuraminic acid in the heterogeneity of alkaline phosphatase in sheep brain, Biochem. J., 107, 185, 1968.

    CAS  Google Scholar 

  537. Brunel, C., Cathala, G., and Saintot, M., Purification et propriétés de la phosphatase alcaline du cerveau de boeuf, Biochim. Biophys. Acta, 7Pi, 621, 1969.

    Google Scholar 

  538. Kirschmann, C., Levy, I., and De Vries, A., Stabilization by cations of microsomal ATPase against heat inactivation, Biochim. Biophys. Acta, 330, 167, 1973.

    CAS  Google Scholar 

  539. Muller, E., Pearse, A. G. E., and Moss, D. W., The inducible alkaline phosphatase of rat heart: Some properties of the enzyme and factors influencing its activity, Biochem. J., 123, 895, 1971.

    CAS  Google Scholar 

  540. Moss, D. W., Muller, E., Pearse, A. G. E., and Thomas, D. M., The inducible alkaline phosphatase of rat heart: Partial purification of the enzyme and its substrate specificity, J. Mol. Cell. Cardiol. 5, 191, 1973.

    CAS  Google Scholar 

  541. Nathanson, L., and Fishman, W. H., New observations on the Regan isoenzyme of alkaline phosphatase in cancer patients, Cancer, 27, 1388, 1971.

    CAS  Google Scholar 

  542. Higashino, K., Hashinotsume, M., Kang, K. Y., Takahashi, Y., and Yamamura, Y., Studies on a variant alkaline phosphatase in sera of patients with hepatocellular carcinoma, Clin. Chim. Acta, 40, 61, 1972.

    Google Scholar 

  543. Inglis, N. R., Kirley, S., Stolbach, L. L., and Fishman, W. H., Phenotypes of the Regan isoenzyme and identity between the placental D-variant and the Nagao isoenzyme, Cancer Res., 33, 1657, 1973.

    CAS  Google Scholar 

  544. Jennings, R. C., Brocklehurst, D., and Hirst, M., A rapid automated screening technique for the detection of placental-like alkaline phosphatase in malignant disease, J. Gin. Pathol., 25, 349, 1972.

    CAS  Google Scholar 

  545. Bowers, B., and Korn, E. D., Cytochemical identification of phosphatase activity in the contractile vacuole of Acanthamoeba castellanii, J. Cell Biol., 59, 784, 1973.

    CAS  Google Scholar 

  546. Saleem, M., and Alikhan, M. A., Characteristics of alkaline phosphatases from the terrestial isopod, Porcellio laevis Latreille (Porcellionidae, Isopoda), Comp. Biochem. Physiol., 4 7B, 307, 1974.

    Google Scholar 

  547. Slinger, I., and Gibson, R., Biochemical observations on the phosphatase enzymes of five species of nemertean worms, Comp. Biochem. Physiol., 47B, 279, 1974.

    CAS  Google Scholar 

  548. Schneiderman, H., Young, W. J., and Childs, B., Patterns of alkaline phosphatase in developing Drosophila, Science, 151, 461, 1966.

    CAS  Google Scholar 

  549. Ayala, F. J., and Tracey, M. L., Genetic differentiation within and between species of the Drosophila willistoni group, Proc. Natl. Acad. Sci. U.S.A., 71, 999, 1974.

    Google Scholar 

  550. Beckman, L., and Johnson, F. M., Genetic variations of phosphatases in larvae of Drosophila melanogaster, Nature (London), 201, 321, 1964.

    CAS  Google Scholar 

  551. Harper, R. A., and Armstrong, F. B., Alkaline phosphatase of Drosophila melanogaster, Biochem. Genet., 10, 29, 1973.

    CAS  Google Scholar 

  552. Horiuchi, T., Horiuchi, S., and Mizuno, D., A possible negative feedback phenomenon controlling formation of alkaline phosphomonoesterase in E. coli, Nature (London), 183, 1529, 1959.

    CAS  Google Scholar 

  553. Torriani, A., Influence of inorganic phosphate on the formation of phosphatases by Escherichia coli, Biochim. Biophys. Acta, 38, 460, 1960.

    CAS  Google Scholar 

  554. Echols, H., Garen, A., Garen, S., and Torriani, A., Genetic control of repression of alkaline phosphatase in E. coli, J. Mol. Biol., J, 425, 1961.

    Google Scholar 

  555. Suzuki, T., and Garen, A., Fragments of alkaline phosphatase from nonsense mutants. 1. Isolation and characterization of fragments from amber and ochre mutants, J. Mol. Biol., 45, 549, 1969.

    CAS  Google Scholar 

  556. Signer, E. R., Non-heritable factors in gene expression, Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, 1963.

    Google Scholar 

  557. Natori, S., and Garen, A., Molecular heterogeneity in the amino-terminal region of alkaline phosphatase, J. Mol. Biol., 49, 511, 1970.

    Google Scholar 

  558. Piggott, P. J., Sklar, M. D., and Gorini, L., Ribosomal alterations controlling alkaline phosphatase isozymes in Escherichia coli, J. Bacteriol., 110, 291, 1972.

    Google Scholar 

  559. Gorini, L., Informational suppression, Annu. Rev. Genet., 4, 107, 1970.

    CAS  Google Scholar 

  560. Pratt, C., and Gallant, J., Growth instability of the alkaline phosphatase repressor, J. Mol. Biol., 75, 433, 1973.

    CAS  Google Scholar 

  561. Levinthal, C., Signer, E. R., and Fetherolf, K., Reactivation and hybridization of reduced alkaline phosphatase, Proc. Natl. Acad. Sci. U.S.A., 48, 1230, 1962.

    CAS  Google Scholar 

  562. Cheng, K. J., Day, D. F., Costerton, J. W., and Ingram, J. M., Alkaline phosphatase subunits in the culture filtrate of Pseudomonas aeruginosa, Can. J. Biochem., 50, 268, 1972.

    CAS  Google Scholar 

  563. Morris, H., and Schlesinger, M. J., Effects of proline analogues on the formation of alkaline phosphatase in Escherichia coli, J. Bacteriol., Ill, 203, 1972.

    Google Scholar 

  564. Schlesinger, M. J., and Olsen, R., A new, simple, rapid procedure for purification of Escherichia coli alkaline phosphatase, Anal. Biochem., 36, 86, 1970.

    CAS  Google Scholar 

  565. Sykes, B. D., Weingarten, H. I., and Schlesinger, M. J., Fluorotyrosine alkaline phosphatase from Escherichia coli: Preparation, properties and fluorine-19 nuclear magnetic resonance spectrum, Proc. Natl. Acad. Sci. U.S.A., 71, 469, 1974.

    CAS  Google Scholar 

  566. Garen, A., and Echols, H., Properties of two regulatory genes for alkaline phosphatase, J.Bacteriol., 83, 297, 1962.

    CAS  Google Scholar 

  567. Garen, A., and Echols, H., Genetic control of induction of alkaline phosphatase synthesis in E. coli, Proc. Natl. Acad. Sci. U.S.A., 48, 1398, 1962.

    CAS  Google Scholar 

  568. Wilkins, A. S., Physiological factors in the regulation of alkaline phosphatase synthesis in Escherichia coli, J. Bacteriol., 110, 616, 1972.

    CAS  Google Scholar 

  569. Anagnostopoulos, C., Alkaline phosphatase formation in B. subtilis, Fed. Proc. Fed. Am. Soc. Exp. Biol., 79, 48, 1960.

    Google Scholar 

  570. Demain, A. L., and Hendlin, D., Phosphohydrolases of a Bacillus subtilis mutant accumulating inosine and hypoxanthine, J. Bacteriol., 94, 66, 1967.

    CAS  Google Scholar 

  571. Chesbro, W. R., and Lampen, J. O., Characteristics of secretion of penicillinase, alkaline phosphatase and nuclease by Bacillus species, J. Bacteriol., 96, 428, 1968.

    CAS  Google Scholar 

  572. Moses, V., The regulatory process in the de-repression of enzyme synthesis: Alkaline phosphatase of Bacillus subtilis, Biochem. J., 103, 650, 1967.

    CAS  Google Scholar 

  573. Ghosh, A., and Ghosh, B. K., Alkaline phosphatase derepression in vegetative cells of Bacillus subtilis by glucose and its reversal by lactate, Biochem. Biophys. Res. Commun., 46, 296, 1972.

    CAS  Google Scholar 

  574. Takeda, K., and Tsugita, A., Phosphoesterases of Bacillus subtilis. II. Crystallization and properties of alkaline phosphatase, J. Biochem. (Tokyo), 61, 231, 1967.

    CAS  Google Scholar 

  575. Glenn, A. R., and Mandelstam, J., Sporulation in Bacillus subtilis 168: Comparison of alkaline phosphatase from sporulating and vegetative cells, Biochem. J., 123, 129, 1971.

    CAS  Google Scholar 

  576. Carrillo-Castañedo, G., and Ortega, M. V., Effect of inorganic phosphate upon Salmonella typhimurium phosphatase activities: Non-repressible alkaline phosphatase and non-inhibited acid phosphatase, Biochim. Biophys. Acta, 146, 535, 1967.

    Google Scholar 

  577. Cheng, K. J., Ingram, J. M., and Costerton, J. W., Release of alkaline phosphatase from cells of Pseudomonas aeruginosa by manipulation of cation concentration and of pH, J. Bacteriol., 104, 748, 1970.

    CAS  Google Scholar 

  578. MacAlister, T. J., Costerton, J. W., Thompson, L., Thompson, J., and Ingram, J. M., Distribution of alkaline phosphatase within the periplasmic space of gram-negative bacteria, J. Bacteriol., Ill, 827, 1972.

    Google Scholar 

  579. Thompson, L. M. M., and MacLeod, R. A., Factors affecting the activity and stability of alkaline phosphatase in a marine pseudomonad, J. Bacteriol., 117, 813, 1974.

    CAS  Google Scholar 

  580. Thompson, L. M. M., and MacLeod, R. A., Biochemical localization of alkaline phosphatase in the cell wall of a marine pseudomonad, J. Bacteriol., 117, 819, 1974.

    CAS  Google Scholar 

  581. Friedberg, I., and Avigad, G., Some properties of alkaline phosphatase of Pseudomonas flúorescens, Eur. J. Biochem., 1, 193, 1967.

    CAS  Google Scholar 

  582. Glew, R. H., and Heath, E. C., Studies on the extracellular alkaline phosphatase of Micrococcus sodonensis. II. Factors affecting secretion, J. Biol. Chem., 246, 1566, 1971.

    CAS  Google Scholar 

  583. Milstein, C., The amino-acid sequence around the reactive serine residue in alkaline phosphatase from Escherichia coli, Biochem. J., 92, 410, 1964.

    CAS  Google Scholar 

  584. Bhatti, A. R., Variation of alkaline phosphatase isoenzymes in Escherichia coli and Serratia marcescens, FEBS Lett., 32, 81, 1973.

    CAS  Google Scholar 

  585. Bhatti, A. R., and Done, J., Antigenic independence of the two types of alkaline phosphatases from Serratia marcescens strain 211, Life Sci., 13, 1421, 1973.

    CAS  Google Scholar 

  586. Kuo, M. H., and Blumenthal, H. J., Purification and properties of an acid phosphomonoesterase from Neurospora crassa, Biochim. Biophys. Acta, 52, 13, 1961.

    CAS  Google Scholar 

  587. Ames, B. N., The biosynthesis of histidine; L-Histidinol phosphate phosphatase, J. Biol. Chem., 226, 583, 1957.

    CAS  Google Scholar 

  588. Kuo, M. H., and Blumenthal, H. J., An alkaline phosphomonoesterase from Neurospora crassa, Biochim. Biophys. Acta, 54, 101, 1961.

    CAS  Google Scholar 

  589. Nyc, J. F., Kadner, R. J., and Crocken, B. J., A repressible alkaline phosphatase in Neurospora crassa, J. Biol. Chem., 241, 1468, 1966.

    CAS  Google Scholar 

  590. Kadner, R. J., and Nyc, J. F., A repressible alkaline phosphatase in Neurospora crassa. III. Enzymatic properties, J. Biol. Chem., 244, 5125, 1969.

    CAS  Google Scholar 

  591. Kuo, M. H., and Blumenthal, H. J., Absence of phosphatase repression by inorganic phosphate in some micro-organisms, Nature (London), 190, 29, 1961.

    CAS  Google Scholar 

  592. Toh-E, A, and Ishikawa, T., Genetic control of synthesis of repressible phosphatases in Neurospora crassa, Genetics 69, 339, 1971

    Google Scholar 

  593. Lehman, J. F., Gleason, M. K., Ahlgren, S. K., and Metzenberg, R. L., Regulation of phosphate metabolism in Neurospora crassa: Chacterization of regulatory mutants, Genetics 75, 61, 1973.

    CAS  Google Scholar 

  594. Dorn, G. L., Purification and characterization of phosphatase I from Aspergillus nidulans, J. Biol. Chem., 243, 3500, 1968.

    CAS  Google Scholar 

  595. Pankovich, A. M., Sclamberg, E. L., and Stevens, J., Organ-specific and cross-reacting isoenzymes in human alkaline phosphatases, Int. Arch. Allergy, 43, 401, 1972.

    CAS  Google Scholar 

  596. Sussman, H. H., Source of the increased serum alkaline phosphatase activity in Paget’s disease, Clin. Chim. Acta, 27, 121, 1970.

    CAS  Google Scholar 

  597. Clinicopathologic Conference: Hypercalcemia and an elevated alkaline phosphatase level, Am. J. Med., 54, 751, 1973.

    Google Scholar 

  598. Allen, R. A., and Friedenwald, J. S., Distribution of substrate-specific alkaline phosphatases in the ocular tissues, Arch. Ophthalmol., 50, 611, 1953.

    Google Scholar 

  599. Petitclerc, C., A kinetic study of heat stability of alkaline phosphatases. Application to sera with normal alkaline phosphatase activities, Clin. Chem., 20, 888, 1974 (Abstract).

    Google Scholar 

  600. Beckman, L., Blood groups and serum alkaline phosphatase, Ser. Haematol., 1, 137, 1968.

    Google Scholar 

  601. Cunningham, V. R., and Rimer, J. G., Isoenzymes of alkaline phosphatase in human serum, Biochem. J., 89, 51P, 1963.

    Google Scholar 

  602. Robinson, J. C., and Goldsmith, L. A., Genetically determined variants of serum alkaline phosphatase: A review, Vox Sang., 13, 289, 1967.

    CAS  Google Scholar 

  603. Arfors, K. E., Beckman, L., and Lundin, L. G., Genetic variations of human serum phosphatases,Acta Genet. 13, 89, 1963.

    CAS  Google Scholar 

  604. Bamford, K. F., Harris, H., Luffman, J. E. Robson, E. B., and Cleghorn, T. E., Serum alkaline phosphatase and the ABO blood groups, Lancet, 1, 530, 1965.

    CAS  Google Scholar 

  605. Walker, B. A., Eze, L. C., Tweedie, M. C. K., and Price Evans, D. A., The influence of ABO blood groups, secretor status and fat ingestion on serum alkaline phosphatase, Clin. Chim. Acta, 35, 433, 1971.

    CAS  Google Scholar 

  606. Langman, M. J. S., Leuthold, E., Robson, E. B., Harris, J., Luffman, J. E., and Harris, H., Influence of diet on the “intestinal” component of serum alkaline phosphatase in people of different ABO blood groups and secretor status, Nature (London), 212, 41, 1966.

    CAS  Google Scholar 

  607. Statland, B. E., Nishi, H. H., and Young, D. S., Serum alkaline phosphatase: Total activity and isoenzyme determinations made by use of the centrifugal fast analyzer, Clin. Chem., 18, 1468, 1972.

    CAS  Google Scholar 

  608. Statland, B. E., Winkel, P., and Bokelund, H., Serum alkaline phosphatase after fatty meals: The effect of substrate on the assay procedure, Clin. Chim. Acta, 49, 299, 1973.

    CAS  Google Scholar 

  609. Keiding, N. R., The alkaline phosphatase fractions of human lymph, Clin. Sci., 26, 291, 1964.

    CAS  Google Scholar 

  610. Blomstrand, R., and Werner, B., Alkaline phosphatase activity in human thoracic duct lymph, Acta Chim. Scand., 129, 111, 1965.

    Google Scholar 

  611. Lum, G., and Gambino, S. R., A comparison of serum versus heparinized plasma for routine chemistry tests, Am. J. Gin. Pathol., 61, 108, 1974.

    CAS  Google Scholar 

  612. Round, J. M., Plasma calcium, magnesium, phosphorus, and alkaline phosphatase levels in normal British school-children, Br. Med. J., 3, 137, 1973.

    CAS  Google Scholar 

  613. Kattwinkel, J., Taussig, L. M., Statland, B. E., and Verier, J. I., The effects of age on alkaline phosphatase and other serologic liver function tests in normal subjects and in patients with cystic fibrosis, J. Pediatr., 82, 234, 1973.

    CAS  Google Scholar 

  614. Shreffler, D. C., Genetic studies of blood group-associated variations in a human serum alkaline phosphatase, Am. J. Hum. Genet., 17, 11, 1965.

    Google Scholar 

  615. Walter, H., Bajatzadeh, M., and Nemeskeri, J., Sex and age relations of alkaline serum phosphatase phenotypes, Hum. Hered., 20, 427, 1970.

    CAS  Google Scholar 

  616. Beckman, L., Associations between human serum alkaline phosphatases and blood groups, Acta Genet., 14, 286, 1964.

    CAS  Google Scholar 

  617. Bodansky, M., Campbell, K., and Ball, E., Changes in serum calcium, inorganic phosphate and phosphatase activity in the pregnant woman, Am. J. Clin. Pathol., 9, 35, 1939.

    Google Scholar 

  618. Boles, J., Leroux, M. L., and Perry, W. F., Investigation of alkaline phosphatase activity in the serum of pregnant rats, Biochim. Biophys. Acta, 261, 197, 1972.

    CAS  Google Scholar 

  619. McMaster, Y., Tennant, R., Clubb, J. S., Neale, F. C., and Posen, S., The mechanism of the elevation of serum alkaline phosphatase in pregnancy, J. Obstet. Gynaecol. Br. Communw., 71, 735, 1964.

    CAS  Google Scholar 

  620. Biswas, S., and Hindocha, P., The serum heat labile alkaline phosphatase activity during pregnancy, Clin. Chim. Acta, 38, 455, 1972.

    Google Scholar 

  621. Watney, P. J. M., and Rudd, B. T., Calcium metabolism in pregnancy and in the newborn, J. Obstet. Gynaecol. Br. Commonw., 81, 210, 1974.

    CAS  Google Scholar 

  622. Aoba, H., Hariu, Y., and Yamaguchi, R., Serum heat-stable alkaline phosphatase in normal and abnormal pregnancy, Tohoku J. Exp. Med., 91, 201, 1967.

    CAS  Google Scholar 

  623. Curzen, P., and Morris, I., Serum alkaline phosphatase in the hypertensive disorders of pregnancy, J. Obstet. Gynaecol. Br. Commonw., 72, 397, 1965.

    CAS  Google Scholar 

  624. Hunter, R. J., Pinkerton, J. H. M., and Johnston, H., Serum placental alkaline phosphatase in normal pregnancy and preeclampsia, Obstet. Gynecol., 36, 536, 1970.

    CAS  Google Scholar 

  625. Elder, M. G., Serum heat-stable alkaline phosphatase levels in normal and abnormal pregnancy, Am. J. Obstet. Gynecol 113, 833, 1972.

    CAS  Google Scholar 

  626. Pirani, B. B. K., MacGillivray, I., and Duncan, R. O., Serum heat stable alkaline phosphatase in normal pregnancy and its relationship to urinary oestriol and pregnanediol excretion, placental weight and baby weight, J. Obstet. Gynaecol. Br. Commonw., 79, 127, 1972.

    CAS  Google Scholar 

  627. Petrucco, O. M., Cellier, K., and Fishtail, A., Diagnosis of intrauterine fetal growth retardation by serial serum oxytocinase, urinary oestrogen and serum heat stable alkaline phosphatase (HSAP) estimations in uncomplicated and hypertensive pregnancies, J. Obstet. Gynaecol. Br. Commonw., 80, 499, 1973.

    CAS  Google Scholar 

  628. Vermehren, E., Plasmaphosphatase während der Gravidität und der Laktation, Acta Med. Scand., 100, 254, 1939.

    CAS  Google Scholar 

  629. Kay, H. D., Some phosphorus compounds of milk. 1. The presence in milk of organic acid- soluble phosphorus compounds, Biochem. J., 19, 433, 1925.

    CAS  Google Scholar 

  630. Bailie, M. J., and Morton, R. K., Comparative properties of microsomes from cow’s milk and from mammary gland. 1. Enzymic activities, Biochem. J., 69, 35, 1958.

    CAS  Google Scholar 

  631. Kay, H. D., Plasma phosphatase. II. The enzyme in disease, particularly in bone disease, J. Biol. Chem., 89, 249, 1930.

    CAS  Google Scholar 

  632. Kerkhoff, J. F., A rapid serum screening test for increased osteoblastic activity, Clin. Chim. Acta, 22, 231, 1968.

    CAS  Google Scholar 

  633. Cadeau, B. J., and Malkin, A., A relative heat stability test for the identification of serum alka¬line phosphatase isoenzymes, Clin. Chim. Acta, 45, 235, 1973.

    CAS  Google Scholar 

  634. Warshaw, J. B., Littlefield, J. W., Fishman, W. H., Inglis, N. R., and Stolbach, L. L., Serum alkaline phosphatase in hypophosphatasia, J. Gin. Invest., 50, 2137, 1971.

    CAS  Google Scholar 

  635. Edlund, Y., and Christoffersson, E., Alkaline phosphatase and transaminases in serum and hepatic duct bile in patients with normal or blocked biliary flow, Acta Hepatosplenol., 14, 230, 1967.

    CAS  Google Scholar 

  636. Ratliff, C. R., Hall, F. F., Culp, T. W., Gevedon, R. F., and Westfall, C. L., The differentiation of hepatic and skeletal alkaline phosphatase by thermofractionation, Am. J. Gastroenterol., 38, 22, 1972.

    Google Scholar 

  637. Sebesta, D. G., Bradshaw, F. J., and Prockop, D. J., Source of the elevated serum alkaline phosphatase activity in biliary obstruction: Studies using isolated liver perfusion, Gastroenterology, 47, 166, 1964.

    CAS  Google Scholar 

  638. Freeman, S., Comparison of effects of hepatectomy and of common bile duct obstruction on serum phosphatase of adult dogs, Am. J. Physiol., 164, 792, 1951.

    CAS  Google Scholar 

  639. Parsons, V., Walker, R. J., and Howorth, P. J. N., Serum 5’-nucleotidase and alkaline phosphatase isoenzymes in diagnosis, with special reference to haemochromatosis, Ann. Gin. Biochem., 10, 179, 1973.

    CAS  Google Scholar 

  640. Caputo, M. J., and Taft, D. M., Separation of serum alkaline phosphatases by micro starch gel electrophoresis, Am. J. Gin. Pathol., 56, 220, 1971.

    CAS  Google Scholar 

  641. Rhone, D. P., White, F. M., and Gidaspow, H., Isoenzymes of liver alkaline phosphatase in serum of patients with hepatobiliary disorders, Clin. Chem., 19, 1142, 1973.

    CAS  Google Scholar 

  642. Afonja, A. O., and Baron, D. N., Plasma alkaline phosphatase isoenzymes in hepatobiliary disease, J. Clin. Pathol., 27, 916, 1974.

    CAS  Google Scholar 

  643. Sundblad, L., Nilsson, M. W., and Brohult, J., Characterization of alkaline phosphatase isoenzymes in serum by agar gel electrophoresis, Clin. Chim. Acta, 45, 219, 1973.

    CAS  Google Scholar 

  644. Brohult, J., and Sundblad, L., Isoenzyme patterns of serum alkaline phosphatase in ethanol- induced liver injury, Acta Med. Scand., 194, 497, 1973.

    CAS  Google Scholar 

  645. Rhone, D. P. Personal communication, 1974.

    Google Scholar 

  646. Fishman, W. H., Inglis, N. I., and Krant, M. J., Serum alkaline phosphatase of intestinal origin in patients with cancer and with cirrhosis of the liver, Clin. Chim. Acta, 12, 298, 1965.

    CAS  Google Scholar 

  647. Stolbach, L. L., Krant, M. J., Inglis, N. I., and Fishman, W. H., Correlation of serum L-phenylalanine-sensitive alkaline phosphatase, derived from intestine, with the ABO blood groups of cirrhotics, Gastroenterology, 52, 819, 1967.

    CAS  Google Scholar 

  648. Warnes, T. W., Hine, P. M., and Kay, G. H., Serum alkaline phosphatase isoenzymes in liver disease, Gut, 13, 853, 1972.

    CAS  Google Scholar 

  649. Gault, M. H., Cohen, M. W., Kahana, L. M., Leelin, F. T., Meakins, J. F., and Aronovitch, M., Serum enzymes in patients with carcinoma of the lung: Lactic acid dehydrogenase, phosphohexose isomerase, alkaline phosphatase and glutamic oxaloacetic transaminase, Can. Med. Assoc. J., 96, 87, 1967.

    CAS  Google Scholar 

  650. Cowan, R. J., and Young, K. A., Evaluation of serum alkaline phosphatase determination in patients with positive bone scans, Cancer, 32, 887, 1973.

    CAS  Google Scholar 

  651. Aisenberg, A. C., Kaplan, M. M., Rieder, S. V., and Goldman, J. M., Serum alkaline phosphatase at the onset of Hodgkin’s disease, Cancer, 26, 318, 1970.

    CAS  Google Scholar 

  652. Pietroni, R. G., An unusual tumour of the spleen associated with a high serum alkaline phosphatase, Guy’s Hosp. Rep., 119, 379, 1970.

    CAS  Google Scholar 

  653. Nakayama, T., Yoshida, M., and Kitamura, M., L-Leucine sensitive, heat stable alkaline phosphatase isoenzyme detected in a patient with pleuritis carcinomatosa, Clin. Chim. Acta, 30, 546, 1970.

    Google Scholar 

  654. Durocher, J. R., Alkaline phosphatase and hypernephroma, N. Engl. J. Med., 281, 1369, 1969.

    CAS  Google Scholar 

  655. Walsh, P. N., and Kissane, J. M., Nonmetastatic hypernephroma with reversible hepatic dysfunction, Arch. Intern. Med., 122, 214, 1968.

    CAS  Google Scholar 

  656. Lemmon, W. T., Holland, P. V., and Holland, J. M., The hepatopathy of hypernephroma, Am. J. Surg., 110, 487, 1965.

    Google Scholar 

  657. Axelsson, V., Hagerstrand, I., and Zettervall, O., Unusual pattern of hepatic alkaline phosphatase activity and renal carcinoma, Acta Med. Scand., 195, 223, 1974.

    CAS  Google Scholar 

  658. Utz, D. C., Warren, M. M., Gregg, J. A., Ludwig, J., and Kelalis, P. P., Reversible hepatic dysfunction associated with hypernephroma, Mayo Gin. Proc., 45, 161, 1970.

    CAS  Google Scholar 

  659. Ariyan, S., Farber, L. R., Hamilton, B. P., and Papac, R. J., Pseudohypoparathyroidism in head and neck tumors, Cancer, 33, 159, 1974.

    CAS  Google Scholar 

  660. Harris, O. D., Warner, M., and Cooke, W. T., Serum alkaline phosphatase in adult coeliac disease, Gut, 10, 655, 1969.

    CAS  Google Scholar 

  661. Garrick, R., Ireland, A. W., and Posen, S., Bone abnormalities after gastric surgery: A prospective histological study, Ann. Intern. Med., 75, 221, 1971.

    CAS  Google Scholar 

  662. Harris, 0. D., Cooke, W. T., Thompson, H., and Waterhouse, J. A., Malignancy in adult celiac disease and idiopathic steatorrhea, Am. J. Med., 42, 899, 1967.

    Google Scholar 

  663. Mistilis, S., and Goulston, S., Liver disease in ulcerative colitis, in: Recent Advances in Gastroenterology (Badenoch, J., and Brooke, B. N., eds.), p. 227, Churchill, London, 1965.

    Google Scholar 

  664. Chapin, L. E., Scudamore, H. H., Baggenstoss, A. H., and Bargen, J. A., Regional enteritis: Associated visceral changes, Gastroenterology, 30, 404, 1956.

    CAS  Google Scholar 

  665. Dordal, E., Glagov, S., and Kirsner, J. B., Hepatic lesions in chronic inflammatory bowel disease. 1. Clinical correlations with liver biopsy diagnoses in 103 patients, Gastroenterology, 52, 239, 1967.

    CAS  Google Scholar 

  666. Eade, M. N., Cooke, W. T., and Williams, J. A., Liver disease in Crohn’s disease: A study of 100 consecutive patients, Scand. J. Gastroenterol., 6, 199, 1971.

    CAS  Google Scholar 

  667. Yong, J. M., Cause of raised serum-alkaline phosphatase after partial gastrectomy and in other malabsorption states, Lancet, 1, 1132, 1966.

    CAS  Google Scholar 

  668. Dent, C. E., Norris, T. S. M., Smith, R., Sutton, R. A. L., and Temperley, J. M., Steatorrhoea with striking increase of plasma alkaline phosphatase of intestinal origin, Lancet, 1, 1333, 1968.

    CAS  Google Scholar 

  669. Pulvertaft, C. N., Luffman, J. E., Robson, E. B., Harris, H., and Langman, M. J. S., Isoenzymes of alkaline phosphatase in patients operated upon for peptic ulcer, Lancet, 1, 237, 1967.

    CAS  Google Scholar 

  670. Dixon, J. A., and Verner, J. L., Enzymes in intestinal strangulation-obstruction, J. Am. Med. Assoc., 200, 1000, 1967.

    CAS  Google Scholar 

  671. Bodansky, A., and Jaffe, H. L., Phosphatase studies. III. Serum phosphatases in diseases of the bone: Interpretation and significance, Arch. Intern. Med., 54, 88, 1934.

    CAS  Google Scholar 

  672. Cassar, J., and Joseph, S., Alkaline phosphatase levels in thyroid disease, Clin. Chim.Acta, 23, 33, 1969.

    CAS  Google Scholar 

  673. Ohlen, J., Pause, H., and Richter, J., Alkaline phosphatase: Diagnostic value of isoenzyme determination, Eur. J. Gin. Invest., 1, 445, 1971.

    CAS  Google Scholar 

  674. Richter, J., and Ohlen, J., Hyperthyreose und die Isoenzyme der alkalischen Phosphatase, Dtsch. Med. Wochenschr., 96, 196, 1971.

    CAS  Google Scholar 

  675. Ohlen, J., and Richter, J., Serumenzymspiegel alkalischer Dunndarmphosphatasen bei der Hyperthyreose, Klin. Wochenschr., 51, 143, 1973.

    CAS  Google Scholar 

  676. Ingham, J. P., Stewart, J. H., and Posen, S., Quantitative skeletal histology in untreated end-stage renal failure, Br. Med. J., 2, 745, 1973.

    CAS  Google Scholar 

  677. Ingham, J. P., Kleerekoper, M., Stewart, J. H., and Posen, S., Symptomatic skeletal disease in non-terminal renal failure, Med. J.Aust., 1, 873, 1974.

    CAS  Google Scholar 

  678. Bishop, M. C., Plasma biochemistry in haemodialyzed patients, Lancet, 2, 1328, 1973.

    CAS  Google Scholar 

  679. Ireland, P., Rashid, A., Von Lichtenberg, F., Cavallo, T., and Merrill, J. P., Liver disease in kidney transplant patients receiving azathioprine, Arch. Intern. Med., 132, 29, 1973.

    CAS  Google Scholar 

  680. Kleerekoper, M., Ibels, L. S., Ingham, J. P., McCarthy, S. W., Mahony, J. F., Stewart, J. H., and Posen, S., Hyperparathyroidism after renal transplantation, Br. Med. J., 3, 680, 1975.

    CAS  Google Scholar 

  681. De Broe, M. E., Bosteels, V., and Wieme, R. J., Increased intestinal alkaline phosphatase in serum of patients on maintenance haemodialysis, Lancet, 1, 753, 1974.

    Google Scholar 

  682. Walker, A. W., Intestinal alkaline phosphatase in serum of patients on maintenance haemodialysis, Clin. Chim. Acta, 55, 399, 1974.

    CAS  Google Scholar 

  683. Winkelman, J., Nadler, S., Demetrious, J., and Pileggi, V. J., The clinical usefulness of alkaline phosphatase determinations, Am. J. Clin. Pathol., 57, 625, 1972.

    CAS  Google Scholar 

  684. Dale, N. E., and Hensley, W. J., Some observations on the heat inactivation of plasma alkaline phosphatase, Pathology, 6, 29, 1974.

    CAS  Google Scholar 

  685. Tadayyon, B., and Lutwak, L., Effects of dietary fats, calcium and phosphorus on rat serum alkaline phosphatases, Proc. Soc. Exp. Biol. Med., 130, 188, 1969.

    CAS  Google Scholar 

  686. Highman, B., and Hanks, A. R., Serum intestinal alkaline phosphatase in rats after 800R whole- body or regional X-irradiation, Proc. Soc. Exp. Biol. Med., 133, 1201, 1970.

    CAS  Google Scholar 

  687. Kang, K. Y., Alkaline phosphatase isozyme in rats with damage in hepatobiliary tract, Tohoku J. Exp. Med., 105, 53, 1971.

    CAS  Google Scholar 

  688. Bussell, N. E., Vogel, J. J. and Levy, B. M., Magnesium deficiency. II. Isoenzymes of serum alkaline phosphatase in acute magnesium deficiency, Proc. Soc. Exp. Biol. Med., 145, 574, 1974.

    CAS  Google Scholar 

  689. Dufour, D., Estrada, R., and Taskar, S. P., Liberation of mouse uterus-specific protein in the serum during uterine carcinogenesis, Cancer Res., 32, 590, 1972.

    CAS  Google Scholar 

  690. Gould, B. S., and Schwachman, H., Bone and tissue phosphatase in experimental scurvy and studies on the source of serum phosphatase, Am. J. Physiol., 135, 485, 1942.

    CAS  Google Scholar 

  691. Cox, R. A., and Gokcen, M., A study of golden hamster (Cricetus cricetus) alkaline phosphatase isoenzymes, Comp. Biochem. Physiol., 46B, 99, 1973.

    CAS  Google Scholar 

  692. Rosenquist, J., Effects of supply and withdrawal of fluoride: Experimental studies, Acta Pathol. Microbiol. Scand. Sect. A, 81, 645, 1973.

    CAS  Google Scholar 

  693. Kramer, J. W., and Sleight, S. D., The isoenzymes of serum alkaline phosphatase in cats, Am. J. Vet. Clin. Pathol, 2, 87, 1968.

    Google Scholar 

  694. Dalgaard, J. B., Phosphatase in cats with obstructive jaundice, Acta Physiol. Scand., 15, 290, 1948.

    CAS  Google Scholar 

  695. Drill, V. A., Annegers, J. H., Snapp, E. F., and Ivy, A. C., Effect of biliary fistula on bromsulphalein retention, serum phosphatase and bile phosphatase, J. Gin. Invest., 24, 97, 1945.

    CAS  Google Scholar 

  696. Marcuson, R. W., and Tomlinson, B., L-Phenylalaine inhibition as a method for measuring the intestinal component of alkaline phosphatase in dog serum, Clin. Chim. Acta, 42, 245, 1972.

    Google Scholar 

  697. Wang, C. C., and Grossman, M. I., Non-excretion of serum alkaline phosphatase by the liver and pancreas of normal dogs, Am. J. Physiol., 156, 256, 1949.

    CAS  Google Scholar 

  698. Bodansky, A., Phosphatase studies. VI. Non osseous origins of serum phosphatase: Its increase after ingestion of carbohydrates, J. Biol. Chem., 104, 473, 1934.

    CAS  Google Scholar 

  699. Bounous, G., and Hugon, J., Serum levels of intestinal alkaline phosphatase in relation to shock, Surgery, 69, 238, 1971.

    CAS  Google Scholar 

  700. Gahne, B., Genetic variation of phosphatase in cattle serum, Nature (London), 199, 305, 1963.

    CAS  Google Scholar 

  701. Gahne, B., Alkaline phosphatase isoenzymes in serum, seminal plasma and tissues of cattle, Hereditas (Lund), 57, 100, 1967.

    CAS  Google Scholar 

  702. Healy, P. J., Isoenzymes of alkaline phosphatase in serum of lambs and ewes, Res. Vet. Sci., 19, 120, 1975.

    CAS  Google Scholar 

  703. Rendei, J., and Stormont, C., Variants of ovine alkaline serum phosphatases and their associ¬ation with the R. O. blood groups, Proc. Soc. Exp. Biol. Med., 115, 853, 1964.

    Google Scholar 

  704. Rasmusen, B. A., Inheritance of R-O-i blood groups and alkaline phosphatase polymorphism in sheep, Genetics, 51, 767, 1965.

    CAS  Google Scholar 

  705. Hope, R. M., Association between serum alkaline phosphatase variants and the R-O-i blood group system in the Australian merino, Aust. J. Biol. Sci., 19, 1171, 1966.

    Google Scholar 

  706. Healy, P. J., Serum alkaline phosphatase in the newborn lamb, Clin. Chim. Acta, 33, 437, 1971.

    CAS  Google Scholar 

  707. Healy, P. J., Isoenzymes of alkaline phosphatase in serum of newly born lambs, Res. Vet. Sci., 19, 127, 1975.

    CAS  Google Scholar 

  708. Hunt, R. D., and Chalifoux, L., Alkaline phosphatase isoenzymes in the squirrel monkey (Saimiri sciureus), Am. J. Vet. Res., 32, 967, 1971.

    CAS  Google Scholar 

  709. Babson, A. L., Greeley, S. J., Coleman, C. M., and Phillips, G. E., Phenolphthalein monophosphate as a substrate for serum alkaline phosphatase, Clin. Chem., 12, 482, 1966.

    CAS  Google Scholar 

  710. Motzok, I., Studies on the plasma phosphatase of normal and rachitic chicks. 3. The assay of antiachitic preparations by a method based on the determination of plasma phosphatase activity, Biochem. J., 47, 196, 1950.

    CAS  Google Scholar 

  711. Wilcox, F. H., Genetic control of serum alkaline phosphatase in the chicken, J. Exp. Zool., 152, 195, 1963.

    CAS  Google Scholar 

  712. Law, G. R. J., Alkaline phosphatase and leucine aminopeptidase association in plasma of the chicken, Science, 156, 1106, 1967.

    CAS  Google Scholar 

  713. Bide, R. W., Plasma alkaline phosphatase in the fowl: Differentiation of tissue isozymes by urea, in: Advances in Automated Analysis, Vol. 3, p. 169, Mediad, White Plains, New York, 1970.

    Google Scholar 

  714. Hurwitz, S., and Griminger, P., The response of plasma alkaline phosphatase, parathyroids and blood and bone minerals to calcium intake in the fowl, J. Nutr., 73, 111, 1961.

    Google Scholar 

  715. Pollard, W. O., Shorb, M. S., and Creek, R. D., Alkaline phosphatase, feathering and bone ash in chicks as affected by hemin, Proc. Soc. Exp. Biol. Med., 112, 478, 1963.

    CAS  Google Scholar 

  716. Motzok, I., and Wynne, A. M., Studies on the plasma phosphatase of normal and rachitic chicks. 1. General characteristics of the enzyme, Biochem. J., 47, 187, 1950.

    CAS  Google Scholar 

  717. Wilson, H. R., and Wilcox, F. H., Origin of an increased serum alkaline phosphatase in chicks, Proc. Soc. Exp. Biol. Med., 113, 413, 1963.

    CAS  Google Scholar 

  718. Stutts, E. C., Briles, W. E., and Kunkel, H. O., Plasma alkaline phosphatase activity in mature inbred chickens, Poultry Sci., 36, 269, 1957.

    CAS  Google Scholar 

  719. Bide, R. W., and Dorward, W. J., Plasma alkaline phosphatase in the fowl: Changes with starvation, Poultry Sci., 49, 708, 1970.

    CAS  Google Scholar 

  720. Savage, T. F., Collins, W. M., and Smith, E. C., Detection of isoenzymes of chicken serum alkaline phosphatase using polyacrylamide disc electrophoresis, Poultry Sci., 50, 740, 1971.

    CAS  Google Scholar 

  721. Roopnarinesingh, S., Morris, D., and Matadial, L., Amniotic fluid heat-stable alkaline phosphatase in normal pregnancy and in pre-eclampsia, J. Obstet. Gynaecol. Br. Commonw., 79, 29, 1972.

    CAS  Google Scholar 

  722. Kellen, J. A., Kaspar, D., and Leung, K. K. Y., Alkaline phosphatase from amniotic fluid, Enzymol Biol. Clin., 11, 429, 1970.

    CAS  Google Scholar 

  723. Sutcliffe, R. G., and Brock, D. J. H., Observations on the origin of amniotic fluid enzymes, J. Obstet. Gynaecol. Br. Commonw., 79, 902, 1972.

    CAS  Google Scholar 

  724. Cornish, C. J., and Posen, S., Human salivary alkaline phosphatase, Clin. Chim. Acta, 20, 387

    Google Scholar 

  725. Sussman, H. H., Evidence that the increased serum alkaline phosphatase activity in patients with osteomalacia or Paget’s disease is from liver phosphatase isoenzyme, c/in. Res., 16, 130, 1968.

    Google Scholar 

  726. McCarty, D. J., Solomon, S. D., Warnock, M. L., and Paloyan, E., Inorganic pyrophosphate concentrations in the synovial fluid of arthritic patients, J. Lab. Clin. Med., 78, 216, 1971.

    CAS  Google Scholar 

  727. Sahani, K. M., Harper, W. J., Jensen, R. G., Parry, R. M., and Zittle, C. A., Enzymes in bovine milk: A review, J. Dairy Sci., 56, 531, 1973.

    Google Scholar 

  728. Morton, R. K., Microsomal particles of normal cow’s milk, Nature (London), 171, 734, 1953.

    CAS  Google Scholar 

  729. Morton, R. K., Alkaline phosphatase of milk. 1. Association of the enzyme with a particulate lipoprotein complex, Biochem. J., 55, 786, 1953.

    CAS  Google Scholar 

  730. Morton, R. K., Alkaline phosphatase of milk. 2. Purification of the enzyme, Biochem. J., 55, 795, 1953.

    CAS  Google Scholar 

  731. Morton, R. K., The substrate specificity and inhibition of alkaline phosphatases of cow’s milk and calf intestinal mucosa, Biochem. J., 61, 232, 1955.

    CAS  Google Scholar 

  732. Sanders, G. P., and Sager, O. S. Modification of the phosphatase test as applied to cheddar cheese and application of the test to fluid milk, J. Dairy Sci., 29, 737, 1946.

    CAS  Google Scholar 

  733. Wright, R. C., and Tramer, J., Reactivation of milk phosphatase following heat treatment. I, J. Dairy Res., 20, 177, 1953.

    CAS  Google Scholar 

  734. Wright, R. C., and Tramer, J., Reactivation of milk phosphatase following heat treatment. I, J. Dairy Res., 20, 258, 1953.

    CAS  Google Scholar 

  735. Richardson, L. A., McFarren, E. F., and Campbell, J. E., Phosphatase reactivation, J. Dairy Sci., 47, 205, 1964.

    CAS  Google Scholar 

  736. Sjöström, G., Swedish investigations concerning milk phosphatase, 12th International Dairy Congress, Stockholm, Papers and Communications, 2, 750, 1949.

    Google Scholar 

  737. Peereboom, J. W. C., and Beekes, H. W., Differentiation of native and renatured alkaline milk phosphatase by means of Sephadex gel thin-layer chromatography, J. Chromatogr., 39, 339

    Google Scholar 

  738. Huggins, C., and Talalay, P., Sodium phenolphthalein phosphate as a substrate for phosphatase tests, J. Biol. Chem., 159, 399, 1945.

    CAS  Google Scholar 

  739. Pasternack, A., Alkaline phosphatase in urine, Scand. J. Clin. Lab. Invest., 16, 145, 1964.

    CAS  Google Scholar 

  740. Raab, W., and Moerth, C., Renal enzyme excretion following administration of analgesic and antirheumatic drugs, Helv. Med. Acta, 37, 73, 1973.

    CAS  Google Scholar 

  741. Wright, P. J., Leathwood, P. D., and Plummer, D. T., Enzymes in rat urine: Alkaline phosphatase, Enzymologia, 42, 317, 1972.

    CAS  Google Scholar 

  742. Warnes, T., Hine, P., and Kay, G., Hormonal influences on intestinal alkaline phosphatase, Gastroenterology, 66, 321, 1974.

    CAS  Google Scholar 

  743. Abul-Fadl, M. A. M., and King, E. J., Purification of faecal alkaline phosphatase, Biochem. J., 44, 431, 1949.

    CAS  Google Scholar 

  744. Eggermont, E., Enzymic activities in meconium from human foetuses and newborns, Biol. Neonat., 10, 266, 1966.

    CAS  Google Scholar 

  745. Horrigan, F. D., and Danovitch, S. H., The origin of human fecal alkaline phosphatase, Am. J. Dig. Dis., 19, 603, 1974.

    CAS  Google Scholar 

  746. Heppel, L. A., and Hilmoe, R. J., Mechanism of enzymic hydrolysis of adenosine triphosphate, J. Biol Chem., 202, 217, 1953.

    CAS  Google Scholar 

  747. Juhn, S. K., Huff, J. S., and Paparella, M. M., Biochemical analyses of middle ear effusions, Ann. Otol., 80, 347, 1971.

    CAS  Google Scholar 

  748. Gordon, F. H., Hyndman, L. A., Bloom, F. C., Anderson, H. D., Taylor, H. L., and McCall, K. B., The preparation and properties of human serum albumin separated from placental extracts, J. Am. Chem. Soc., 75, 5859, 1953.

    CAS  Google Scholar 

  749. Posen, S., Clubb, J. S., Neale, F. C., and Hotchkis, D., The measurement of plasma volume by enzyme dilution, J. Lab. Gin. Med., 65, 530, 1965.

    CAS  Google Scholar 

  750. Beckman, G., Genetics of human placental alkaline phosphatases, Ph.D. thesis, University of Umea, Sweden, 1970.

    Google Scholar 

  751. Timperley, W. R., Alkaline-phosphatase-secreting tumour of lung, Lancet, 2, 356, 1968.

    CAS  Google Scholar 

  752. Timperley, W. R., and Warnes, T. W., Alkaline phosphatase in meningiomas, Cancer (Philadelphia), 26, 100, 1970.

    CAS  Google Scholar 

  753. Rendel, J., Aalund, O., Freedland, R. A., and Moller, F., The relationship between the alkaline phosphatase polymorphism and blood group O in sheep, Genetics, 50, 973, 1964.

    CAS  Google Scholar 

  754. LeVeen, H. H., Talbot, L. J., Restuccia, M., and Barberio, J. R., Metabolism and excretion of alkaline phosphatase in relation to liver function and determination of maximal secretory rates of liver, J. Lab. Clin. Med., 36, 192, 1950.

    Google Scholar 

  755. Bengmark, S., and Olsson, R., Elimination of alkaline phosphatase from serum in dog after intravenous injection of canine phosphatases from bone and intestine, Acta Chir. Scand., 140, 1, 1974.

    CAS  Google Scholar 

  756. International Union of Biochemistry, Report of the Commission on Enzymes, Pergamon Press, Oxford, 1961.

    Google Scholar 

  757. Mendicino, J., and Vasarhely, F., Renal D-fructose-l,6-diphosphatase, J. Biol. Chem., 238, 3528, 1963.

    CAS  Google Scholar 

  758. Kirtley, M. E., and Dix, J., The hydrolysis of phosphoenol pyruvate catalyzed by rabbit liver fructose-1,6-diphosphatase, Biochem. Biophys. Res. Commun., 37, 634, 1969.

    CAS  Google Scholar 

  759. Chou, T., and Kirtley, M. E., p-Nitrophenylphosphate as substrate for rabbit liver fructose diphosphatase, Biochem. Biophys. Res. Commun., 45, 98, 1971.

    CAS  Google Scholar 

  760. King, E. J., The enzymic hydrolysis of lecithin, Biochem. J., 25, 799, 1931.

    CAS  Google Scholar 

  761. Albers, R. W., Rodriguez de Lores Arnaiz, G., and De Robertis, E., Sodium-potassium-activated ATPase and potassium activated p-nitrophenylphosphatase: A comparison of their subcellular localizations in the rat brain, Proc. Natl. Acad. Sci. U.S.A., 53, 557, 1965.

    Google Scholar 

  762. Yoshida, H., Izumi, F., and Nagai, K., Carbamylphosphate, a preferential substrate of K+- dependent phosphatase, Biochim. Biophys. Acta, 120, 183, 1966.

    CAS  Google Scholar 

  763. Nagai, K., Izumi, F., and Yoshida, H., Studies on potassium-dependent phosphatase; its distribu¬tion and properties, J. Biochem. (Tokyo), 59, 295, 1966.

    CAS  Google Scholar 

  764. Fujita, M., Nakao, T., Tashima, Y., Mizuno, N., Nagano, K., and Nakao, M., Potassium-ion stimulated p-nitrophenylphosphatase activity occurring in a highly specific adenosine triphosphatase preparation from rabbit brain, Biochim. Biophys. Acta., 117, 42, 1966.

    CAS  Google Scholar 

  765. Emmelot, P., and Bos, C. J., On the participation of neuraminidase-sensitive sialic acid in the K+-dependent phosphohydrolysis of p-nitrophenylphosphate by isolated rat liver plasma membranes, Biochim. Biophys. Acta., 115, 244, 1966.

    CAS  Google Scholar 

  766. Rao, G. J. S., Del Monte, M., and Nadler, H. L., K+ -activated, ethacrynic acid-sensitive p- nitrophenyl phosphatase from normal human white cells, Biochim. Biophys. Acta, 235, 454, 1971.

    CAS  Google Scholar 

  767. Cotterrell, D., and Whittam, R., An increase in p-nitrophenylphosphate hydrolysis by human red cell membranes on lowering ionic strength,J. Physiol., 219,22P, 1971.

    Google Scholar 

  768. Knuuttila, M. L. E., and Makinen, K. K., Purification and characterization of a phosphatase specifically hydrolyzing p-nitrophenyl phosphate from an oral strain of Streptococcus mutans, Arch. Biochem. Biophys., 152, 685, 1972.

    CAS  Google Scholar 

  769. Attias, J., Bonnet, J. L., and Sauvagnargues, J. C., Séparation et étude partielle de deux phosphatases alcalines de levure, Biochim. Biophys. Acta, 212, 315, 1970.

    CAS  Google Scholar 

  770. Smith, A. F., and Fogg, B. A., Possible mechanisms for the increase in alkaline phosphatase activity of lyophilized control material, Clin. Chem., 18, 1518, 1972.

    CAS  Google Scholar 

  771. Granstrom, G., and Linde, A., A comparative study of alkaline phosphatase in calcifying cartilage, odontoblasts and the enamel organ, Calcif. Tissue Res., 22, 231, 1977.

    CAS  Google Scholar 

  772. Smithies, O., Zone electrophoresis in starch gels: Group variations in the serum proteins of normal human adults, Biochem. J., 61, 629, 1955.

    CAS  Google Scholar 

  773. Sandler, M., and Bourne, G. H., Starch gel electrophoresis of alkaline phosphatases using a histochemical method, Nature (London), 194, 389, 1962.

    CAS  Google Scholar 

  774. Allen, J. M., and Hynick, G. J., Localization of alkaline phosphatase in gel matrices following electrophoresis, J. Histoehem. Cytochem., 11, 169, 1963.

    CAS  Google Scholar 

  775. Usategui-Gomez, M., Yeager, F. M., and Tarbutton, P., Purification of human placental alkaline phosphatase by isoelectric focusing, Clin. Chim. Acta, 50, 405, 1974.

    CAS  Google Scholar 

  776. Greene, P. J., and Sussman, H. H., Structural comparison of ectopic and normal placental alkaline phosphatase, Proc. Natl. Acad. Sci. U.S.A., 70, 2936, 1973.

    CAS  Google Scholar 

  777. Khattab, M., and Pfleiderer, G., Alkaline phosphatase of human and calf small intestine: Purification and immunochemical characterization, Z. Physiol. Chem., 357, 377, 1976.

    CAS  Google Scholar 

  778. Everett, R. M., Duncan, J. R., and Prasse, K. W., Alkaline phosphatases in tissues and sera of cats, Am. J. Vet. Res., 38, 1533, 1977.

    CAS  Google Scholar 

  779. Findlay, A. B., and Johnston, N. G., The isoenzyme of alkaline phosphatase in neutrophils during pregnancy, Pathology, 9, 13, 1977.

    CAS  Google Scholar 

  780. Moriuchi, S., and DeLuca, H. F., The effect of vitamin D3 metabolites on membrane proteins of chick duodenal brush borders, Arch. Biochem. Biophys., 174, 367, 1976.

    CAS  Google Scholar 

  781. Luduena, M. A., Iverson, G. M., and Sussman, H. H., Expression of liver and placental alkaline phosphatases in Chang liver cells, J. Cell. Physiol., 91, 119, 1977.

    CAS  Google Scholar 

  782. DeBroe, M. E., and Wieme, R. J., The cholestatic doublet of alkaline phosphatase: Its origin and clinical significance, in: Isozymes, Vol. Ill, Developmental Biology (Markert, C. L., ed.), p. 799, Academic Press, New York, 1975.

    Google Scholar 

  783. Bloch, W., and Schlesinger, M. J., Kinetics of substrate hydrolysis of molecular variants of Escherichia coli alkaline phosphatase, J. Biol. Chem., 249, 1760, 1974.

    CAS  Google Scholar 

  784. Bosron, W. F., and Vallee, B. L., Effect of phosphate on multiple forms of Escherichia coli alkaline phosphatase, Biochem. Biophys. Res. Commun., 66, 809, 1975.

    CAS  Google Scholar 

  785. Harvey, D. G., and Obeid, H. M. A., Some properties of alkaline phosphatase in dog tissues and serum, Br. Vet. J., 130, 489, 1974.

    CAS  Google Scholar 

  786. Bretaudiere, J. P., Vassault, A., Amsellem, L., Pourci, M. L., Thieu-Phung, H., and Bailly, M., Criteria for establishing a standardized method for determinating alkaline phosphatase activity in human serum, Clin. Chem., 23, 2263, 1977.

    CAS  Google Scholar 

  787. Halton, D. W., Studies on phosphatase activity in trematoda, J. Parasitol., 53, 46, 1967.

    CAS  Google Scholar 

  788. Elser, R. C., Serum alkaline phosphatase measured by using thymol blue monophosphate and a bichromate analyzer, Clin. Chem., 22, 1737, 1976.

    CAS  Google Scholar 

  789. Neumann, H., Klein, E., Hauck-Granoth, R., Yachnin, S., and Ben-Bassat, H., Comparative study of alkaline phosphatase activity in lymphocytes, mitogen-induced blasts, lymphoblastoid cell lines, acute myeloid leukemia and chronic lymphatic leukemia cells, Proc. Natl. Acad. Sci. U.S.A., 73, 1432, 1976.

    CAS  Google Scholar 

  790. McWhinnie, D. J., and Saunders, J. W., Developmental patterns and specificities of alkaline phosphatase in the embryonic chick limb, Dev. Biol., 14, 169, 1966.

    CAS  Google Scholar 

  791. Brockman, R. W., and Heppel, L. A., On the localization of alkaline phosphatase and cylic phosphodiesterase in Escherichia coli, Biochemistry, 7, 2554, 1968.

    CAS  Google Scholar 

  792. Harvey, D. G., The estimation of serum alkaline phosphatase in the dog, J. Small. Anim. Pract., 5, 557, 1967.

    Google Scholar 

  793. Kumar, A., and Christian, G. D., Determination of serum alkaline phosphatase by amperometric measurements of rate of oxygen depletion in a polyphenol oxidase coupled reaction, Anal. Chem., 48, 1283, 1976.

    CAS  Google Scholar 

  794. Harris, H., Hopkinson, D. A., and Robson, E. B., The incidence of rare alleles determining electrophoretic variants: Data on 43 enzyme loci in man, Ann. Hum. Genet. (London), 37, 237, 1974.

    CAS  Google Scholar 

  795. McComb, R. B., and Bowers, G. N., Jr., Study of optimum buffer conditions for measuring alkaline phosphatase activity in human serum, Clin. Chem., 18, 97, 1972.

    CAS  Google Scholar 

  796. Van Belle, H., Kinetics and inhibition of rat and avian alkaline phosphatases, Gen. Pharmacol., 7, 53, 1976.

    Google Scholar 

  797. Belfanti, S., Contardi, A., and Ercoli, A., Studies on the phosphatase: The influence of some electrolytes on the phosphatases of animal tissues: Phosphatases of the liver, kidney, serum and bones of the rabbit, Biochem. J., 29, 517, 1935.

    CAS  Google Scholar 

  798. Belfanti, S., Contardi, A., and Ercoli, A., Researches on the phosphatases, Biochem. J., 29, 1491, 1935.

    CAS  Google Scholar 

  799. Common, R. H., Serum phosphatase in the domestic fowl, J. Agric. Sci., 26, 492, 1936.

    CAS  Google Scholar 

  800. Garlich, J. D., Chicken serum alkaline phosphatase: Application of a kinetic assay and investigation of phenylalanine and homoarginine as selective inhibitors, Poultry Sci., 53, 957, 1974.

    CAS  Google Scholar 

  801. Ruegnitz, P. C., and Schwartz, E., Effects of chemical inhibition of alkaline phosphatase isoenzymes in the dog, Am. J. Vet. Res., 32, 1525, 1971.

    CAS  Google Scholar 

  802. Manning, J. P., Inglis, N. R., Green, S., and Fishman, W. H., Characterization of placental alkaline phosphatase from the rabbit, guinea pig, mouse, and hamster, Enzymologia, 39, 307, 1970.

    CAS  Google Scholar 

  803. Kadlecovä, L., and Stépan, J., Phosphatases. VI. pH dependence of the organ-specific thermostability of alkaline phosphatases in tissue homogenates, Experientia, 28, 1284, 1972.

    Google Scholar 

  804. Fishman, W. H., and Sie, H. G., Organ specific inhibition of human alkaline phosphatase isoenzymes of liver, bone, intestine and placenta: L-Phenylalanine, L-tryptophane and L-homo- arginine, Enzymologia, 41, 141, 1971.

    CAS  Google Scholar 

  805. Dobozy, A., and Hammer, H., Some properties of alkaline phosphatase in Bacillus species, Acta Microbiol. Acad. Sci. Hung., 16, 181, 1969.

    CAS  Google Scholar 

  806. Cathala, G., Brunel, C., Chappelet-Tordo, D., and Lazdunski, M., Bovine kidney alkaline phosphatase: Catalytic properties, subunit interactions in the catalytic process, and mechanism of Mg2+ stimulation, J. Biol. Chem., 250, 6046, 1975.

    CAS  Google Scholar 

  807. Borgers, M., The cytochemical application of new potent inhibitors of alkaline phosphatase, J. Histochem. Cytochem., 21, 812, 1973.

    CAS  Google Scholar 

  808. Zittle, C. A., and Della Monica, E. S., Effect of aliphatic alcohols on bovine alkaline phosphatase, Arch. Biochem. Biophys., 37, 419, 1952.

    CAS  Google Scholar 

  809. Mather, I. H., and Keenan, T. W., The stability of alkaline phosphatase in sodium dodecyl sulfate, FEBS Lett., 44, 79, 1974.

    CAS  Google Scholar 

  810. Schlesinger, M. J., Bloch, W., and Kelley, P. M., Differences in structure, function and formation of two isozymes of Escherichia coli alkaline phosphatase, in: Isozymes I: Molecular Structure (Markert, C. L., ed.), p. 333, Academic Press, New York, 1975.

    Google Scholar 

  811. Burton, E. G., and Metzenberg, R. L., Properties of a repressible alkaline phosphatase from wild type and a wall-less mutant of Neurospora crassa, J. Biol. Chem., 249, 2679, 1974.

    Google Scholar 

  812. Komoda, T., and Sakagishi, Y., Partial purification and some properties of human liver alkaline phosphatase, Biochim. Biophys. Acta, 438, 138, 1976.

    CAS  Google Scholar 

  813. Komoda, T., and Sakagishi, Y., Partial purification of human intestinal alkaline phosphatase with affinity chromatography, Biochim. Biophys. Acta, 445, 645, 1976.

    CAS  Google Scholar 

  814. Bloch, W., and Schlesinger, M. J., The phosphate content of Escherichia coli alkaline phosphatase and its effect on stopped flow kinetic studies, J. Biol. Chem, 248, 5794, 1973.

    CAS  Google Scholar 

  815. Chappelet-Tordo, D., Lazdunski, C., Iwatsubo, M., and Lazdunski, M., The non-equivalence of the active sites and the mechanism of a mutationally altered E. coli alkaline phosphatase, Biochem. Biophys. Res. Commun., 63, 529, 1975.

    CAS  Google Scholar 

  816. Cox, R. P., Ghosh, N. K., Bazzell, K., and Griffin, M. J., Hormonally induced modification of the HeLa alkaline phosphatase with increased catalytic activity, in Isozymes I: Molecular Structure (Markert, C. L., ed.), p. 343, Academic Press, New York, 1975.

    Google Scholar 

  817. Tanabe, Y., and Wilcox, F. H., Effects of age, sex, and line on serum alkaline phosphatase of the chicken, Proc. Soc. Exp. Biol. Med., 103, 68, 1960.

    CAS  Google Scholar 

  818. Wiese, A. C., Johnson, B. C., Elvehjem, C. A., Hart, E. B., and Halpin, J. G., A study of blood and bone phosphatase in chick perosis, J. Biol. Chem., 127, 411, 1939.

    CAS  Google Scholar 

  819. Skillen, A. W., and Pierides, A. M., Serum alkaline phosphatase isoenzyme patterns in patients with chronic renal failure, Clin. Chim. Acta, 80, 339, 1977.

    CAS  Google Scholar 

  820. McWhinnie, D. J., Oeltgen, P. R., and Stiles, D., Amphibian alkaline phosphatase. I. Biochemical characterization of alkaline phosphatase in tissues of Rana pipiens, Comp. Biochem. Physiol., 38B, 247, 1971.

    CAS  Google Scholar 

  821. Danielli, J. F., A critical study of techniques for determining the cytological position of alkaline phosphatase, J. Exp. Biol., 22, 110, 1946.

    CAS  Google Scholar 

  822. Pearse, A. G. E., Histochemistry, Theory and Applied, 3rd ed., p. 510, Churchill, London, 1968.

    Google Scholar 

  823. Majno, G., and Rouiller, C., Die alkalische Phosphatase in der Biologie des Knochengewebes: Histochemische Untersuchungen, Virchows Arch. Pathol. Anat. Physiol, 321, 1, 1951.

    CAS  Google Scholar 

  824. Kirschmann, C., Levy, I., and DeVries, A., Stabilization by cations of microsomal ATPase against heat inactivation, Biochim. Biophys. Acta, 330, 167, 1973.

    CAS  Google Scholar 

  825. Cornish, C., and Posen, S., Unpublished observations, 1973.

    Google Scholar 

  826. Hofstee, B. H. J., Alkaline phosphatase. I. Mechanism of action of Zn, Mg, glycine, versene and hydrogen ions, Arch. Biochem. Biophys., 59, 352, 1955.

    CAS  Google Scholar 

  827. Petitclerc, C., Quantitative fractionation of alkaline phosphatase isoenzymes according to their thermostability, Clin. Chem., 22, 42, 1976.

    CAS  Google Scholar 

  828. Dixon, M., and Webb, E. C., Enzymes, 2nd ed., p. 146, Academic Press, New York, 1964.

    Google Scholar 

  829. Wilcox, F. H., A recessively inherited electrophoretic variant of alkaline phosphatase in chicken serum, Genetics, 53, 799, 1966.

    CAS  Google Scholar 

  830. Yeh, M. F., and Trela, J. M., Purification and characterization of a repressible alkaline phosphatase from Thermus aquaticus, J. Biol. Chem., 251, 3134, 1976.

    CAS  Google Scholar 

  831. Lyons, R. B., and Weaver, D. D., Alkaline phosphatase studies on the adult and embryonic stages of the sea urchin, Strongylocentrotus purpuratus,Anat. Rec., 145, 255, 1963.

    Google Scholar 

  832. Probert, A. J., and Lwin, T., Kinetic properties and location of nonspecific phosphomonoesterases in subcellular fractions of Fasciola hepatica, Exp. Parasitol., 35, 253, 1974.

    CAS  Google Scholar 

  833. Metz, M., Pinsky, A., and Wilkinson, J. H., The inhibitory effect of the urea-urease system on human tissue alkaline phosphatases, Clin. Chim. Acta, 30, 325, 1970.

    CAS  Google Scholar 

  834. Cloetens, R., Inactivation reversible de la phosphatase alcaline II en milieu acide, Arch. Intern. Pharmacodyn. Ther., 68, 419, 1942.

    CAS  Google Scholar 

  835. Mathies, J. C., Preparation and properties of highly purified alkaline phosphatase from swine kidneys, J. Biol. Chem., 233, 1121, 1958.

    CAS  Google Scholar 

  836. Probert, A. J., Goil, M. M., and Sharma, R. K., Biochemical and histochemical studies on the non-specific phosphomonesterases of Fasciola gigantica cobbold 1855, Parasitology, 64, 347, 1972.

    CAS  Google Scholar 

  837. Savage, T. F., Collins, W. M., and Smith, E. C., Onset of egg production and its relationship to isoenzymes of serum alkaline phosphatase in Japanese quail, Poultry Sci., 49, 1662, 1970.

    CAS  Google Scholar 

  838. Savage, T. F., Collins, W. M., and Smith, E. C., Serum alkaline phosphatase isoenzymes in Japanese quail, Poultry Sci., 49, 1435, 1970.

    Google Scholar 

  839. Erasmus, D. A., Studies on phosphatase systems of cestodes. II. Studies on Cysticercus tenio- collis and Moniezia expansa (adult), Parasitology, 47, 81, 1957.

    CAS  Google Scholar 

  840. Posen, S., and Brudenell-Woods, J., Unpublished observations, 1967.

    Google Scholar 

  841. Belfanti, S., Contaidi, A., and Ercoli, A., Researches on the phosphatases. II. Inactivation and reactivation of the phosphatases of animal origin, Biochem. J., 29, 842, 1935.

    CAS  Google Scholar 

  842. Fishman, W. H., Manning, J. P., Takeda, D. A., and Green, S., Quantitation of potency of antisera to placental alkaline phosphatase by an automated immunoenzyme technique, Anal. Biochem., 51, 368, 1973.

    CAS  Google Scholar 

  843. Lehmann, F. G., Immunological methods for human placental alkaline phosphatase (Regan isoenzyme), Clin. Chim. Acta, 65, 111, 1975.

    Google Scholar 

  844. Lehmann, F. G., Immunological relationship between human placental and intestinal alkaline phosphatase, Clin. Chim. Acta, 65, 257, 1975.

    CAS  Google Scholar 

  845. Franseen, C. C., and McLean, R., The phosphatase activity of tissues and plasma in tumors of bone, Am. J. Cancer, 24, 299, 1935.

    CAS  Google Scholar 

  846. Walton, R. J., Preston, C. J., Russell, R. G. G., and Kanis, J. A., An estimate of the turnover rate of bone-derived plasma alkaline phosphatase in Paget’s disease, Clin. Chim. Acta, 63, 227, 1975.

    CAS  Google Scholar 

  847. Roche, J., and Sarles, H., Sur la nature et l’origine de la phosphomonoesterase alcaline du sérum, C. R. Soc. Biol, 147, 1858, 1953.

    CAS  Google Scholar 

  848. Aono, H., and Otsuji, N., Genetic mapping of regulator gene phoS for alkaline phosphatase in Escherichia coli J. Bacteriol., 95, 1182, 1968.

    CAS  Google Scholar 

  849. Schlesinger, M. J., and Barrett, K., The reversible dissociation of the alkaline phosphatase of Escherichia coli. I. Formation and reactivation of subunits, J. Biol. Chem., 240, 4284, 1965.

    CAS  Google Scholar 

  850. Reid, T. W., and Wilson, I. B., E. coli alkaline phosphatase, in: The Enzymes, 3rd ed., Vol. 4 (Boyer, P. D., ed.), p. 373, Academic Press, New York, 1971.

    Google Scholar 

  851. Meighen, E., and Yue, R., Hybrids of chemical derivatives of Escherichia coli alkaline phosphatase, Biochim. Biophys. Acta, 412, 262, 1975.

    CAS  Google Scholar 

  852. Liu, P. V., Differentiation of pathogenic pseudomonads by heat resistance of alkaline phosphatase, Am. J. Clin. Pathol., 45, 639, 1966.

    Google Scholar 

  853. Dorn, G., and Rivera, W., Kinetics of fungal growth and phosphatase formation in Aspergillus nidulans, J. Bacteriol., 92, 1618, 1966.

    CAS  Google Scholar 

  854. Dorn, G. L., Purification of two alkaline phosphatases from Aspergillus nidulans, Biochim. Biophys. Acta, 132, 190, 1967.

    CAS  Google Scholar 

  855. Solomon, E. P., Johnson, E. M., and Gregg, J. H., Multiple forms of enzymes in a cellular slime mold during morphogenesis, Dev. Biol., 9, 314, 1964.

    CAS  Google Scholar 

  856. O’Day, D. H., and Francis, D. W., Patterns of alkaline phosphatase activity during alternative developmental pathways in the cellular slime mold Polysphondylium pallidum, Can. J. Zool., 51, 301, 1973.

    Google Scholar 

  857. Lipman, H. J., A contribution to the study of phosphatase activity in marine invertebrate animals, Bull. Pittsburgh Univ., 36, 175, 1940.

    Google Scholar 

  858. Stewart, B., and Lakshmanan, S., Some properties of the acid phosphatase and the alkaline phosphatase of the summer jellyfish of the Chesapeake Bay, Chrysaora quinquecirrha desor, Comp. Biochem. Physiol. A, 50, 319, 1975.

    CAS  Google Scholar 

  859. Nimmo-Smith, R. H., and Standen, O. D., Phosphomonoesterases of Schistosoma mansoni, Exp. Parasitol., 13, 305, 1963.

    CAS  Google Scholar 

  860. Dike, S. C., and Read, C. P., Relation of tegumentary phosphohydrolase and sugar transport in Hymenolepis diminuta,J. Parasitol., 57, 1251, 1971.

    CAS  Google Scholar 

  861. Bullock, W. L., Histochemical studies on the Acanthocephala. III. Comparative histochemistry of alkaline phosphatase, Exp. Parasitol., 7, 51, 1958.

    CAS  Google Scholar 

  862. Norris, E. R., and Rama Rao, D. A. R., Phosphatases of marine invertebrates, J. Biol. Chem., 108, 783, 1935.

    CAS  Google Scholar 

  863. Umemori-Aikawa, Y., An alkaline phosphatase in the clam Meretrix meretrix lusoria (Gmelin), with affinities for nucleotides, Comp. Biochem. Physiol. B, 40, 347, 1971.

    CAS  Google Scholar 

  864. Michelson, E. H., and Dubois, L., Increased alkaline phosphatase in the tissues and hemolymph of the snal Biomphalaria glabrata infected with Schistosoma mansoni, Comp. Biochem. Physiol., 44B, 763, 1973.

    CAS  Google Scholar 

  865. Muller, R., Histochemical localization of phosphatases and esterases in Australorbis glabratus, Proc. Zool. Soc. (London), 144, 229, 1965.

    CAS  Google Scholar 

  866. Varute, A. T., and Patil, V. A., Histochemical analysis of molluscan stomach and intestinal alkaline phosphatase: A sialoglycoprotein, Histochemie, 25, 77, 1971.

    CAS  Google Scholar 

  867. Saleem, M., and Alikhan, M. A., Phosphomonoesterases of the digestive gut in Porcellio laevis Latreille (Porcellionidae, Isopoda), Comp. Biochem. Physiol, 45B, 911, 1973.

    CAS  Google Scholar 

  868. Denuce, J. M., Phosphatases and esterases in the digestive gland of the crayfish (Orconectes virilis), Arch. Int. Physiol. Biochim., 75, 159, 1967.

    CAS  Google Scholar 

  869. Bianchi, U., and Pirodda, G., Enzyme interactions in homogenates of parthenogenetic Artemia salina: Alterations of the electrophoretic patterns of some alkaline phosphomonoesterases, Rev. Biol., 61, 585, 1968.

    Google Scholar 

  870. Lauga, J., Etude par électrophorèse de l’évolution des phosphatases alcalines de l’hémolymphe au cours des stades terminaux du développement postembryonnaire du Grillon domestique Acheta domesticus L., C. R. Acad. Sci. Ser. D, 274, 1357, 1972.

    CAS  Google Scholar 

  871. Eguchi, M., Alkaline phosphatase isoenzymes in the alimentary canal of the silkworm, in Isozymes I: Molecular Structure (Markert, C., ed.), p. 315, Academic Press, New York, 1975.

    Google Scholar 

  872. Lakshmi, M. B., Kundra, S., Rao, R. H., and Subrahmanyam, D., Alkaline phosphatase of Culex pipiens fatigans,Indian J. Biochem. Biophys., 10, 99, 1973.

    CAS  Google Scholar 

  873. Hodgson, E., and Kumar, S. S., Alkaline Phosphomonoesterase activity in insects. 2. Activity in various cell fractions from the blow fly Pharmia regina, Ann. Entomol. Soc. Am., 57, 613, 1964.

    CAS  Google Scholar 

  874. Rockstein, M., and Herron, P. W., Phosphatase in the adult worker honey bee, J. Cell. Comp. Physiol, 38, 451, 1951.

    CAS  Google Scholar 

  875. Ludwig, D., Fiore, C., and Jones, C. R., Physiological comparisons between offspring of the yellow mealworm, Tenebrio molitor, obtained from young and from old parents, Ann. Entomol Soc. Am., 55, 439, 1962.

    CAS  Google Scholar 

  876. Fitzgerald, L. R., The alkaline phosphatase of the developing grasshopper egg, J. Exp. Zool., 110. 461, 1949.

    CAS  Google Scholar 

  877. Danielli, J. F., and Catcheside, D. G., Phosphatase on chromosomes, Nature (London), 156, 294, 1945.

    CAS  Google Scholar 

  878. Pfohl, R. J., Changes in alkaline phosphatase during the early development of the sea urchin, Arbacia punctulata, Exp. Cell Res., 39, 496, 1965.

    CAS  Google Scholar 

  879. Pfohl, R. J., Alkaline phosphatase of sea urchin embryos: Chromatographic and electrophetic characterization, Dev. Biol., 44, 333, 1975.

    CAS  Google Scholar 

  880. College of American Pathologists, Systematized Nomenclature of Pathology, 1st ed., p. 1, Chicago, 1965.

    Google Scholar 

  881. Hinsch, G. W., Alkaline phosphatase of the developing down feather: Substrates, activators and inhibitors, Dev. Biol., 2, 21, 1960.

    CAS  Google Scholar 

  882. Jacoby, F., and Martin, B. F., The histochemical test for alkaline phosphatase, Nature (London), 163, 875, 1949.

    CAS  Google Scholar 

  883. Lustig, V., and Kellen, J. A., Fructose 1, 6-diphosphatase activity in rat mammary glands, Comp. Biochem. Physiol, 42B, 703, 1972.

    CAS  Google Scholar 

  884. Mitus, W. J., Mednicoff, I. B., and Dameshek, W., Alkaline phosphatase of mature neutrophils in various polycythemias, N. Engl. J. Med., 260, 1131, 1959.

    CAS  Google Scholar 

  885. Helmy, F. M., Yaeger, R. G., and Hack, M. H., Some histochemical observations on the blood cells of six species of turtles, Comp. Biochem. Physiol, 29, 1281, 1969.

    CAS  Google Scholar 

  886. Kouvalainen, K., Species and organ dependence of alkaline phosphatase activity in lymphatic tissues: A histochemical, biochemical, and electrophoretic study, Histochem. J., 3, 55, 1971.

    CAS  Google Scholar 

  887. Kadner, R. J., Nyc, J. F., and Brown, D. M., A repressible alkaline phosphatase in Neurospara crassa. Biol. Chem., 243, 3076, 1968.

    CAS  Google Scholar 

  888. Albers, H., and Albers, E., Über die Nierenphosphatase. I. Mitteilung zur Kenntnis der Phosphatasen, Z. Physiol. Chem., 132, 165, 1935.

    Google Scholar 

  889. Wachsmuth, E. D., and Hiwada, K., Alkaline phosphatase from pig kidney: Method of purification and molecular properties, Biochem. J., 141, 273, 1974.

    CAS  Google Scholar 

  890. Fosset, M., Chappelet-Tordo, D., and Lazdunski, M., Intestinal alkaline phosphatase: Physical properties and quaternary structure, Biochemistry, 13, 1783, 1974.

    CAS  Google Scholar 

  891. Posen, S., Unpublished observations, 1970.

    Google Scholar 

  892. Dabich, D., and Neuhaus, O. W., The source of synovial fluid alkaline phosphatase, Proc. Soc. Exp. Biol Med., 123, 584, 1966.

    CAS  Google Scholar 

  893. Ohkubo, A., Langerman, N., and Kaplan, M. M., Rat liver alkaline phosphatase: Purification and properties, J. Biol. Chem., 249, 7174, 1974.

    CAS  Google Scholar 

  894. Kind, C. A., and Macchi, M. E., Phosphatase activity in the tissue of the frog, Rana pipiens, J. Cell. Physiol, 39, 153, 1952.

    CAS  Google Scholar 

  895. King, E. J., and Delory, G. E., The rates of enzymatic hydrolysis of phosphoric esters, Biochem. J., 33, 1185, 1939.

    CAS  Google Scholar 

  896. Nitowsky, H. M., Herz, F., and Geller, S., Induction of alkaline phosphatase in dispersed cell cultures by changes in osmolarity, Biochim. Biophys. Res. Commun., 12, 293, 1963.

    CAS  Google Scholar 

  897. Dorner, J. L., Hoffmann, W. E., and Long, G. B., Corticosteroid induction of an isoenzyme of alkaline phosphatase in the dog, Am. J. Vet. Res., 35, 1457, 1974.

    CAS  Google Scholar 

  898. Hoffmann, W. E., and Dorner, J. L., A comparison of canine normal hepatic alkaline phosphatase and variant alkaline phosphatase of serum and liver, Clin. Chim. Acta, 62, 131, 1975.

    Google Scholar 

  899. Mackenzie, A. S. E., Tooth phosphatase, Br. Dent. J., 54, 153, 1933.

    CAS  Google Scholar 

  900. Morse, A., and Greep, R. O., Alkaline glycerophosphatase in the developing teeth of the rat: Its location and activity characteristics as influenced by pH of the substrate and length of incubation, Anat. Rec., 99, 379, 1947.

    CAS  Google Scholar 

  901. Granstrom, G., and Linde, A., A biochemical study of alkaline phosphatase in isolated rat incisor odontoblasts, Arch. Oral Biol., 17, 1213, 1972.

    CAS  Google Scholar 

  902. Magnusson, B. C., Heyden, G., and Arwill, T., Histochemical studies on alkaline phosphatases in mineralizing oral tissues in the mouse, Calcif. Tissue Res., 16, 169, 1974.

    CAS  Google Scholar 

  903. Hodson, A. W., Latner, A. L., and Masterton, J. B., A comparative study of the alkaline phosphatase of the dental pulp, bone and liver using starch gel electrophoresis, Arch. Oral Biol, 10, 547, 1965.

    CAS  Google Scholar 

  904. Woltgens, J. H. M., Bonting, S. L., and Bijvoet, O. L. M., Relationship of inorganic pyrophosphatase and alkaline phosphatase activities in hamster molars, Calcif. Tissue Res., 5, 333, 1970.

    CAS  Google Scholar 

  905. Petersen, D. R., Nelms, G. E., and Anderson, A. D., Serum alkaline phosphatase isoenzymes in beef cattle, Proc. Annu. Meet. Am. Soc. Anim. Sci. West. Sect., 26, 196, 1975.

    CAS  Google Scholar 

  906. Etzler, M. E., and Moog, F., Biochemical identification and characterization of multiple forms of alkaline phosphatase in the developing duodenum of the mouse, Dev. Biol., 18, 515, 1968.

    CAS  Google Scholar 

  907. Davies, M. I., and Motzok, I., Intestinal phosphatase and phytase of chicks: Separation of isoenzymes, zinc contents and in vitro effects of zinc, Comp. Biochem. Physiol., 42B, 345, 1972.

    CAS  Google Scholar 

  908. Brenna, O., Perrella, M., Pace, M., and Pietta, P. G., Affinity-chromatography purification of alkaline phosphatase from calf intestine, Biochem. J., 15 7, 291, 1975.

    Google Scholar 

  909. Lovtrup, S., Synthesis of alkaline phosphatase during the embryonic development of Rana platyrrhinus,Acta Embryol. Morphol. Exp., 2, 54, 1958.

    CAS  Google Scholar 

  910. Savage, D. C., Personal communication, 1975.

    Google Scholar 

  911. Hiwada, K., and Wachsmuth, E. D., Catalytic properties of alkaline phosphatase from pig kidney, Biochem. J., 141, 283, 1974.

    CAS  Google Scholar 

  912. Ramasamy, I., and Butterworth, P. J., Subunit structure and catalytic activity of pig kidney alkaline phosphatase, Biochim. Biophys. Acta, 370, All, 1974.

    Google Scholar 

  913. Hiwada, K., and Wachsmuth, E. D., Alkaline phosphatase from pig kidney: Microheterogeneity and the role of neuraminic acid, Biochem. J., 141, 293, 1974.

    CAS  Google Scholar 

  914. Cathala, G., Brunei, C., Chappelet-Tordo, D., and Lazdunski, M., Bovine kidney alkaline phosphatase: Purification, subunit structure, and metalloenzyme properties, J. Biol. Chem., 250, 6040, 1975.

    CAS  Google Scholar 

  915. Keller, P., Personal communication, 1975.

    Google Scholar 

  916. Jones, H. W., McKusick, V. A., Harper, P. S., and Wuu, K. D., George Otto Gey (1899-1970): The HeLa cell and a reappraisal of its origin, Obstet. Gynecol, 38, 945, 1971.

    Google Scholar 

  917. Maio, J. J., and deCarli, L., Induction and repression of alkaline phosphatase in human cultured cells by prednisolone, hydrocortisone and organic monophosphates, Biochem. Biophys. Res. Commun., 11, 335, 1963.

    CAS  Google Scholar 

  918. Spencer, T., and Macrae, D. L., Some properties of the alkaline phosphatase of HeLa cells, Enzymologia, 42, 329, 1972.

    CAS  Google Scholar 

  919. Fishman, W. H., and Singer, R. M., Placental alkaline phosphatase: Regulation of expression in cancer cells, Ann. N. Y. Acad. Sci., 259, 261, 1975.

    CAS  Google Scholar 

  920. Nakayama, T., and Kitamura, M., L-Leucine sensitive alkaline phosphatase isoenzyme from cancer tissue, Ann. N. Y. Acad. Sci., 259, 325, 1975.

    Google Scholar 

  921. Holmgren, P. A., and Stigbrand, T., Purification and partial characterization of two genetic variants of placental alkaline phosphatase, Biochem. Genet., 14, 111, 1976.

    Google Scholar 

  922. Doellgast, G., Beckman, G., and Beckman, L., On the identity of the “D-variant” with L-leucine sensitive phenotypes of human placental alkaline phosphatase, Clin. Chim. Acta, 75, 501, 1977.

    CAS  Google Scholar 

  923. Edlow, J. B., Ota, T., Relacion, J. R., Kohler, P. O., and Robinson, J. C., Enzymes of normal and malignant trophoblast: Phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase, Am. J. Obstet. Gynecol, 121, 674, 1975.

    CAS  Google Scholar 

  924. Higashino, K., Kudo, S., Ohtani, R., Yamamura, Y., Honda, T., and Sakurai, J., A hepatoma- associated alkaline phosphatase, the Kasahara isozyme, compared with one of the isozymes of FL amnion cells, Ann. N. Y. Acad. Sci., 259, 337, 1975.

    CAS  Google Scholar 

  925. Petitclerc, C., Delisle, M., Martel, M., Fecteau, C., and Brière, N., Mechanism of action of Mg2+ and Zn2+ on rat placental alkaline phosphatase. I. Studies on the soluble Zn2+ and Mg2+ alkaline phosphatases, Can. J. Biochem., 53, 1089, 1975.

    CAS  Google Scholar 

  926. Cunningham, V. R., and Field, E. J., Alkaline phosphatase isoenzyme systems of the guinea pig in health and in experimental allergic encephalomyelitis, J. Neurochem., 11, 281, 1964.

    CAS  Google Scholar 

  927. Balestrieri, C., Colonna, G., Irace, G., and Cedrangolo, F., Purification and some properties of an alkaline phosphatase from beef brain, Comp. Biochem. Physiol, 5 OB, 203, 1975.

    Google Scholar 

  928. Fishman, W. H., Immunologic and biochemical approaches to alkaline phosphatase isoenzyme analysis: The Regan isoenzyme, Ann. N. Y. Acad. Sci., 166, 745, 1969.

    CAS  Google Scholar 

  929. Greene, P. J., and Sussman, H. H., Structural comparison of ectopic and normal placental alkaline phosphatase, Proc. Natl Acad. Sci. U.S.A., 70, 2936, 1973.

    CAS  Google Scholar 

  930. Portugal, M. L., Azevedo, M. S., and Manso, C., Serum alpha-feto-protein and variant alkaline phosphatase in human hepatocellular carcinoma, Int. J. Cancer, 6, 383, 1970.

    CAS  Google Scholar 

  931. Masuzawa, M., Kamada, T., Sakoyama, Y., Ogita, Z., and Ito, F., Detection of carcinoplacental alkaline phosphatase by thin-layer Polyacrylamide gel electrophoresis, Ann. N. Y. Acad. Sci., 259, 321, 1975.

    CAS  Google Scholar 

  932. Suzuki, H., Iino, S., Endo, Y., Torii, M., Miki, K., and Oda, T., Tumor-specific alkaline phosphatase in hepatoma, Ann. N. Y. Acad. Sci., 259, 307, 1975.

    CAS  Google Scholar 

  933. Etzler, M. E., and Moog, F., Inactive alkaline phosphatase in duodenum of nursling mouse: Im¬munological evidence, Science, 154, 1037, 1966.

    CAS  Google Scholar 

  934. Breuer, J., and Stucky, W., Enzymaktivitäten im Serum und Plasma von Mensch, Hund, und Ratte sowie deren Veränderungen beim Aufbewahren des Blutes, Z. Klin. Chem. Klin. Biochem., 13, 355, 1975.

    CAS  Google Scholar 

  935. Harris, E., and Mehl, J. W., Zone electrophoresis of intestinal alkaline phosphatase, Proc. Soc. Exp. Biol Med., 90, 521, 1955.

    CAS  Google Scholar 

  936. Posen, S., Unpublished observations, 1968.

    Google Scholar 

  937. Whitby, L. G., and Moss, D. W., Analysis of heat inactivation curves of alkaline phosphatase isoenzymes in serum, Clin. Chim. Acta, 59, 361, 1975.

    CAS  Google Scholar 

  938. Concustell-Bas, E., Torrents-Pont, J., and Villar-Palasi, V., Localizacion de enzymas en las fracciones proteinicas de la sangre. II. Fosfatasas, Rev. Esp. Fisiol., 19, 25, 1963.

    CAS  Google Scholar 

  939. Lorentz, K., Flatter, B., and Heydrich, D., Disk-electrophorese multipler Formen alkalischer Phosphatasen: Untersuchungen über alkalische Phosphatasen menschlicher Gewebe. I. Mitteilung, Z. Klin. Chem. Klin. Biochem., 12, 81, 1974.

    CAS  Google Scholar 

  940. Arfors, K. E., Beckman, L., and Lundin, L. G., Further studies on the association between human serum phosphatases and blood groups, Acta Genet., 13, 366, 1963.

    CAS  Google Scholar 

  941. Beckman, L., and Grivea, M., Serum alkaline phosphatase variations in pregnant women and newborn children, Acta Genet. (Basel), 15, 218, 1965.

    CAS  Google Scholar 

  942. McComb, R. B., Fundamentals of the chemistry of alkaline phosphatase and their relation to the measurement of alkaline phosphatase activity in the laboratory, in: Proceedings of the Second International Symposium on Clinical Enzymology (Tietz, N. W., Weinstock, A., and Rodgerson, D. O., eds.), p. 27, American Association for Clinical Chemistry, Washington, D.C., 1976.

    Google Scholar 

  943. Cornish, C., and Posen, S., Unpublished observations, 1973.

    Google Scholar 

  944. Nagamine, M., and Ohkuma, S., Serum alkaline phosphatase isoenzymes linked to immunoglobulin G, Clin. Chim. Acta, 65, 39, 1975.

    CAS  Google Scholar 

  945. Ohlen, J., and Richter, J., Das Isoenzymverteilungsmuster alkalischer Serumphosphatasen bei verschiedenen Verlaufsformen der Hepatitis, Med. Klin., 71, 292, 1976.

    CAS  Google Scholar 

  946. Mahony, J. F., Hayes, J. M., Ingham, J. P., and Posen, S., Hypophosphataemic osteomalacia in patients receiving haemodialysis, Br. Med. J., 2, 142, 1976.

    CAS  Google Scholar 

  947. Beckman, L., and Nilson, L. R., Variations of serum enzyme in bird species and hybrids, Hereditas, 53, 221, 1965.

    CAS  Google Scholar 

  948. Baker, C. M. A., Manwell, C., Labisky, R. F., and Harper, J. A., Molecular genetics of avian proteins. V. Egg, blood, and tissue proteins of the ring-necked pheasant, Phasianus colchicus, Comp. Biochem. Physiol, 17, 467, 1966.

    CAS  Google Scholar 

  949. Arsenis, C., Rudolph, J., and Hackett, M. H., Resolution, purification and characterization of the orthophosphate releasing activities from fracture callus calcifying cartilage, Biochim. Biophys. Acta, 391, 301, 1975.

    CAS  Google Scholar 

  950. Arsenis, C., Hackett, M. H., and Huang, S. M., Resolution, specificity and transphosphorylase activity of calcifying cartilage alkaline phosphatases, Calcif Tissue Res., 20, 159, 1976.

    CAS  Google Scholar 

  951. Nakayama, T., and Kitamura, M., L-Leucine sensitive alkaline phosphatase isozyme from cancer tissue, Ann. N. Y. Acad. Sci, 259, 325, 1975.

    Google Scholar 

  952. Johnson, F. M., Developmental differences of alkaline phosphatase zymograms from Drosophila melanogaster and D. ananassae, Nature (London), 272, 843, 1966.

    Google Scholar 

  953. Masayama, T., and Shuto, M., Über die Wirkung der Phosphatase im Krebsgewebe der Leber, Gann, 34, 176, 1940.

    CAS  Google Scholar 

  954. Jimenez-Marin, D., Enzyme inheritance in the laboratory rat: Genetics of a heart aromatic esterase and plasma alkaline phosphatase in substrains of Rattus norvegicus, J. Hered., 65, 235, 1974.

    CAS  Google Scholar 

  955. Segre, A., Richmond, R. C., and Wiley, R. H., Isozyme polymorphism in the ruff (Aves, Philomachus pugnax): A species with polymorphic plumage, Comp. Biochem. Physiol., 36, 589, 1970.

    CAS  Google Scholar 

  956. Moss, D. W., Isoenzymes of alkaline phosphatase in autolysed and butanol-extracted liver preparations, Nature (London), 193, 981, 1962.

    CAS  Google Scholar 

  957. Nayudu, P. R. V., and Hercus, F. B., Molecular heterogeneity of mouse duodenal alkaline phosphatase, Biochem. J., 141, 93, 1974.

    CAS  Google Scholar 

  958. Hoffmann, W. E., and Dorner, J. L., Disappearance rates of intravenously injected canine alkaline phosphatase isoenzymes, Am. J. Vet. Res., 38, 1553, 1977.

    CAS  Google Scholar 

  959. Karpas, A., Hayhoe, F. G. J., Greenberger, J., and Neumann, H., Alkaline phosphatase in Epstein-Barr viral nuclear antigen positive cell lines, Science, 202, 318, 1978.

    CAS  Google Scholar 

  960. Korhonen, L. K., Hamalainen, M., and Kaivosoja, M., Inorganic pyrophosphatase activity distinct from alkaline phosphatase in rat bone, Clin. Orthop. Relat. Res., 128, 332, 1977.

    CAS  Google Scholar 

  961. Mulivor, R. A., Plotkin, L. I., and Harris, H., Differential inhibition of the products of the human alkaline phosphatase loci, Ann. Hum. Genet. (London), 42, 1, 1978.

    CAS  Google Scholar 

  962. MacAlister, T. J., Irvin, R. T., and Costerton, J. W., Immunocytological investigation of protein synthesis in Escherichia coli, J. Bacteriol., 130, 329, 1977.

    CAS  Google Scholar 

  963. Hoffmann, W. E., Renegar, W. E., and Dorner, J. L., Serum half-life of intravenously injected intestinal and hepatic alkaline phosphatase isoenzymes in the cat, Am. J. Vet. Res., 38, 1637, 1977.

    CAS  Google Scholar 

  964. Komoda, T., and Sakagishi, Y., The function of carbohydrate moiety and alteration of carbohydrate composition in human alkaline phosphatase isoenzymes, Biochim. Biophys. Acta, 523, 395, 1978.

    CAS  Google Scholar 

  965. Singh, I., and Tsang, K. Y., An in vitro production of bone specific alkaline phosphatase, Exp. Cell Res., 95, 347, 1975.

    CAS  Google Scholar 

  966. Singh, I., Tsang, K. Y., and Blakemore, W. S., Placenta-like alkaline phosphatases from human osteosarcoma cells, Cancer Res., 38, 193, 1978.

    CAS  Google Scholar 

  967. Wooton, A. M., Neale, G., and Moss, D. W., Some properties of alkaline phosphatases in parenchymal and biliary tract cells separated from rat liver, Clin. Chim. Acta, 61, 183, 1975.

    Google Scholar 

  968. Kanis, J. A., Ernshaw, M., Heynen, G., Ledingham, J. G. G., Oliver, D. O., Russell, R. G. G., Woods, C. G., Franchimont, P., and Gasper, S., Changes in histological and biochemical indexes of bone turnover after bilateral nephrectomy in patients on hemodialysis, M Engl J. Med., 296, 1073, 1977.

    CAS  Google Scholar 

  969. Cleeve, H. J. W., and Brown, I. R. F., Plasma 25-hydroxyvitamin D and alkaline phosphatase isoenzymes in hyperthyroidism, Ann. Gin. Biochem., 15, 320, 1978.

    CAS  Google Scholar 

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McComb, R.B., Bowers, G.N., Posen, S. (1979). Isoenzymes. In: Alkaline Phosphatase. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2970-1_8

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