Measurement of Alkaline Phosphatase Activity

  • Robert B. McComb
  • George N. BowersJr.
  • Solomon Posen

Abstract

This chapter will discuss some practical aspects of alkaline phosphatase assays. While the remarks are based predominantly on experience gained with human blood serum, many of the points raised are also applicable to the assay of alkaline phosphatases from other sources.

Keywords

Alkaline Phosphatase Alkaline Phosphatase Activity Serum Alkaline Phosphatase Nicotinamide Adenine Dinucleotide Phosphate Amino Alcohol 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    McCollum, E. V., and Hart, E. B., On the occurrence of a phytin-splitting enzyme in animal tissues, J. Biol Chem., 4, 497, 1908.Google Scholar
  2. 2.
    Plimmer, R. H. A., The metabolism of organic phosphorus compounds Their hydrolysis by the action of enzymes, Biochem. J., 7, 43, 1913.Google Scholar
  3. 3.
    Kay, H. D., Plasma phosphatase. I. Method of determination. Some properties of the enzyme, J. Biol Chem., 89, 235, 1930.Google Scholar
  4. 4.
    Jenner, H. D., and Kay, H. D., Plasma phosphatase. III. A clinical method for the determination of plasma phosphatase, Br. J. Exp. Pathol., 13, 22, 1932.Google Scholar
  5. 5.
    Bodansky, A., Phosphatase studies. II. Determination of serum phosphatase Factors influencing the accuracy of the determination, J. Biol Chem., 101, 93, 1933.Google Scholar
  6. 6.
    King, E. J., and Armstrong, A. R., A convenient method for determining serum and bile phosphatase activity, Can. Med. Assoc. J., 31, 376, 1934.Google Scholar
  7. 7.
    Ohmori, Y., Uber die Phosphomonoesterase, Enzymologia, 4, 217, 1937.Google Scholar
  8. 8.
    Buch, I., and Buch, H., An improved King and Armstrong method for the determination of phosphatase activity in blood serum, Acta Med. Scand., 101, 211, 1939.Google Scholar
  9. 9.
    Shinowara, G. Y., Jones, L. M., and Reinhart, H. L., The estimation of serum inorganic phos-phate and “acid” and “alkaline” phosphatase activity, J. Biol. Chem., 142, 921, 1942.Google Scholar
  10. 10.
    Huggins, C., and Talalay, P., Sodium phenolphthalein phosphate as a substrate for phosphatase tests, J. Biol Chem., 159, 399, 1945.Google Scholar
  11. 11.
    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.Google Scholar
  12. 12.
    Seligman, A. M., Chauncey, H. H., Nachlas, M. M., Manheimer, L. H., and Ravin, H. A., The colorimetric determination of phosphatases in human serum, J. Biol Chem., 190, 7, 1951.Google Scholar
  13. 13.
    Brandenberger, H., and Hanson, R., Eine spektrophotometrische Bestimmungsmethode fur sauere und alkalische Phosphatases Helv. Chim. Acta, 36, 900, 1953.Google Scholar
  14. 14.
    Marsh, W. H., Fingerhut, B., and Kirsch, E., Adaptation of an alkaline phosphatase method for automatic colorimetric analysis, Clin. Chem., 5, 119, 1959.Google Scholar
  15. 15.
    Garen, A., and Levinthal, C., A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase, Biochim. Biophys. Acta, 38, 470, 1960.Google Scholar
  16. 16.
    Moss, D. W., Kinetics of phosphatase action on naphthyl phosphates, determined by a highly sensitive spectrofluorimetric technique, Biochem J., 76, 32P, 1960.Google Scholar
  17. 17.
    Morgenstern, S., Kessler, G., Auerbach, J., Flor, R. V., and Klein, B., An automated p-nitro- phenylphosphate serum alkaline phosphatase procedure for the Auto Analyzer, Clin. Chem., 77, 876, 1965.Google Scholar
  18. 18.
    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.Google Scholar
  19. 19.
    Bowers, G. N., Jr., and McComb, R. B., A continuous spectrophotometry method for measuring the activity of serum alkaline phosphatase, Clin. Chem., 12, 70, 1966.Google Scholar
  20. 20.
    Hausamen, T. U., Helger, R., Rick, W., and Gross, W., Optimal conditions for the determination of serum alkaline phosphatase by a new kinetic method, Clin. Chim Acta, 15, 241, 1967.Google Scholar
  21. 21.
    Johnson, R. B., Jr., A new fluorometric method for the estimation or detection of total and fractionated alkaline phosphatase, Clin. Chem., 15, 108, 1969.Google Scholar
  22. 22.
    Cornish, C. J., Neale, F. C., and Posen, S., An automated fluorometric alkaline phosphatase microassay with 4-methyl-umbelliferyl phosphate as a substrate, Am J. Clin. Pathol., 53, 68, 1970.Google Scholar
  23. 23.
    Vaughan, A., Guilbault, G. G., and Hackney, D., Fluorometric methods for analysis of acid and alkaline phosphatase, Anal. Chem., 43, 721, 1971.Google Scholar
  24. 24.
    Davidsohn, I., and Nelson, D. A., The blood, in Todd-Sanford Clinical Diagnosis by Laboratory Methods, 15th ed. (Davidsohn, I., and Henry, J. B., eds.), p. 100, W. B. Saunders, Philadelphia, 1974.Google Scholar
  25. 25.
    Statland, B. E., Bokelund, H., and Winkel, P., Factors contributing to intra-individual variation of serum constituents. 4. Effects of posture and tourniquet application on variation of serum constituents in healthy subjects, Clin. Chem., 20, 1513, 1974.Google Scholar
  26. 26.
    Bokelund, H., Winkel, P., and Statland, B. E., Factors contributing to intra-individual variation of serum constituents. 3. Use of randomized duplicate serum specimens to evaluate sources of analytical error, Clin. Chem., 20, 1507, 1974.Google Scholar
  27. 27.
    Winkel, P., Statland, B. E., and Bokelund, H., The effects of time of venipuncture on variation of serum constituents, Am J. Clin. Pathol., 64, 433, 1975.Google Scholar
  28. 28.
    Breuer, J., and Stucky, W., Enzymaktivitäten in Serum und Plasma von Mensch, Hund und Ratte sowie deren Veränderungen beim Aufbewahren des Blutes, Z. Klin. Chem Klin. Biochem., 75, 355, 1975.Google Scholar
  29. 29.
    Lum, G., and Gambino, S. R., A comparison of serum versus heparinized plasma for routine chemistry tests, Am. J. Clin. Pathol., 61, 108, 1974.Google Scholar
  30. 30.
    Evered, D. F., and Steenson, T. I., Citrate inhibition of alkaline phosphatase, Nature (London), 202, 491, 1964.Google Scholar
  31. 31.
    Mollison, P. L., Blood Transfusion in Clinical Medicine, 5th ed., p. 687, Blackwell, Oxford, 1972.Google Scholar
  32. 32.
    Belfanti, S., Contardi, A., and Ercoli, A., Studies on the phosphatases-The influence of some electrolytes on the phosphatases of animal tissue Phosphatases of the liver, kidney, serum and bones of the rabbit, Biochem. J., 29, 517, 1935.Google Scholar
  33. 33.
    Ahmed, Z., and King, E. J., Kinetics of placental alkaline phosphatase, Biochim. Biophys. Acta, 45, 581, 1960.Google Scholar
  34. 34.
    Heppel, L., Harkness, D. R., and Hilmoe, R. J., A study of the substrate specificity and other properties of alkaline phosphatase of Escherichia coli, J. Biol Chem., 237, 841, 1962.Google Scholar
  35. 35.
    Dabich, D., and Neuhaus, O. W., Purification and properties of bovine synovial fluid alkaline phosphatase, J. Biol Chem., 241, 415, 1966.Google Scholar
  36. 36.
    Bitar, K., and Reinhold, J. G., Phytase and alkaline phosphatase activities in intestinal mucosae of rat, chicken, calf and man, Biochim. Biophys. Acta, 268, 442, 1972.Google Scholar
  37. 37.
    Plocke, D. J., and Vallee, B. L., Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents, Biochemistry, 1, 1039, 1962.Google Scholar
  38. 38.
    Friedberg, I., and Avigad, G., Some properties of alkaline phosphatase of Pseudomonas fluo- rescens, Eur. J. Biochem., 1, 193, 1967.Google Scholar
  39. 39.
    Conyers, R. A. J., Birkett, D. J., Neale, F. G, Posen, S., and Brudenell-Woods, J., The action of EDTA on human alkaline phosphatases, Biochim. Biophys. Acta, 139, 363, 1967.Google Scholar
  40. 40.
    Myers, L. J., and Pierce, K. R., Effect of EDTA anticoagulant on enzyme activity and pH of blood, Southwest. Vet., 25, 287, 1972.Google Scholar
  41. 41.
    Brydon, W. G., and Roberts, L. B., The effect of haemolysis on the determination of plasma constituents, Clin. Chim. Acta, 41, 435, 1972.Google Scholar
  42. 42.
    Babson, A. L., The interference of bilirubin in serum phosphatase assays using the substrate p-nitrophenyl phosphate, Am. J. Med. Technol., 28, 227, 1962.Google Scholar
  43. 43.
    Martland, M., and Robison, R., The possible significance of hexose-phosphoric esters in ossification The bone phosphatase. Part VII, Biochem. J., 21, 665, 1927.Google Scholar
  44. 44.
    Torriani, A., Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli, Biochim. Biophys. Acta, 38, 460, 1960.Google Scholar
  45. 45.
    Hilliard, S. D., O’Donnell, J. F., and Schenker, S., On the nature of the inhibitor of urinary alkaline phosphatase, Clin. Chem., 11, 570, 1965.Google Scholar
  46. 46.
    Tietz, N. W., Bayse, D. D., Copeland, W., Duncan, P., Rinker, A. D., Rost, K. J., Vanderlinde, R. E., and Zygowicz, E. R., Selection of reaction conditions for the measurement of alkaline phosphatase activity, in Second International Symposium on Clinical Enzymology (Tietz, N. W., Weinstock, A., and Rodgerson, D. O., eds.), p. 51, American Association for Clinical Chemistry, Washington, D.C., 1976.Google Scholar
  47. 47.
    Bowers, G. N., Jr., Kelley, M. L., and McComb, R. B., Precision estimates in clinical chemistry. 1. Variability of analytic results in a survey reference sample related to the use of a nonhuman serum alkaline phosphatase, Clin. Chem., 13, 595, 1967.Google Scholar
  48. 48.
    Cornish, C. J., and Posen, S., Human salivary alkaline phosphatase, Clin. Chim. Acta, 20, 387, 1968.Google Scholar
  49. 49.
    Amador, E., Zimmerman, T. S., and Wacker, W. E. G, Urinary alkaline phosphatase activity. II. An analytical validation of the assay method, J. Am. Med. Assoc., 185, 953, 1963.Google Scholar
  50. 50.
    Altman, P. L., Blood and Other Body Fluids (Dittmer, D. S., ed.), Federation of American Societies for Experimental Biology, Washington, D.C., 1961.Google Scholar
  51. 51.
    Helve, O., On blood phosphorus distribution in certain internal diseases, Acta.Med. Scand., 125, 505, 1946.Google Scholar
  52. 52.
    Zittle, C. A., and Della Monica, E. S., Effect of aliphatic alcohols on bovine alkaline phosphatases, Arch. Biochem. Biophys., 37, 419, 1952.Google Scholar
  53. 53.
    Krishnaswamy, M., and Kenkare, U. W., The effect of pH, temperature, and organic solvents on the kinetic parameters of Escherichia coli alkaline phosphatase, J. Biol. Chem., 245, 3956, 1970.Google Scholar
  54. 54.
    Brestkin, A. P., and Novitskaya, N. A., Effect of aliphatic alcohols on the hydrolysis of sodium phenyl phosphate by alkaline phosphatase, Biokhimiya, 38, 682, 1973 (in Russian).Google Scholar
  55. 55.
    Kay, H. D., The phosphatases of mammalian tissues, Biochem. J., 22, 855, 1928.Google Scholar
  56. 56.
    Albers, H., and Albers, E., Über die Nierenphosphatase. 1. Mitteilung zur Kenntnis der Phosphatasen, Z. Physiol Chem., 232, 165, 1935.Google Scholar
  57. 57.
    Gamble, J. L., Chemical Anatomy, Physiology and Pathology of Extracellular Fluid, 6th ed., Harvard University Press, Cambridge, Massachusetts, 1964.Google Scholar
  58. 58.
    Fendley, T. W., Hochholzer, J. M., and Fringes, C. S., Effect of various diluents on the activity of several enzymes present in serum, Clin. Chem., 19, 1079, 1973.Google Scholar
  59. 59.
    Wilson, I. B., Dayan, J., and Cyr, K., Some properties of alkaline phosphatase from Escherichia coli, J. Biol. Chem., 239, 4182, 1964.Google Scholar
  60. 60.
    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.Google Scholar
  61. 61.
    Applebury, M. L., Johnson, B. P., and Coleman, J. E., Phosphate binding to alkaline phosphatase Metal ion dependence, J. Biol. Chem., 245, 4968, 1970.Google Scholar
  62. 62.
    Haiford, S. E., Escherichia coli alkaline phosphatase An analysis of transient kinetics, Biochem. J., 125, 319, 1971.Google Scholar
  63. 63.
    Faulkner, W. R., and King, J. W., Renal function, in Fundamentals of Clinical Chemistry (Tietz, N. W., ed.), p. 975, W. B. Saunders, Philadelphia, 1976.Google Scholar
  64. 64.
    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., 727, 470, 1967.Google Scholar
  65. 65.
    Bahr, M., and Wilkinson, J. H., Urea as a selective inhibitor of human tissue alkaline phosphatases, Clin. Chim. Acta, 7 7, 367, 1967.Google Scholar
  66. 66.
    Neumann, H., and Van Vreedendaal, M., An improved alkaline phosphatase determination with p-nitrophenyl phosphate, Clin. Chim. Acta, 7 7, 183, 1967.Google Scholar
  67. 67.
    Armstrong, M. D., and Low, N. L., Phenylketonuria. VIII. Relation between age, serum phenylalanine level and phenylpyruvic acid excretion, Proc. Soc. Exp. Biol. Med., 94, 142, 1957.Google Scholar
  68. 68.
    Fishman, W. H., Green, S., and Inglis, N. I., L-Phenylalanine An organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase, Nature (London), 198, 685, 1963.Google Scholar
  69. 69.
    Raab, W., and Mörth, C., Inhibition of alkaline phosphatase activity by D-penicillamine, Z. Klin. Chem. Klin. Biochem., 12, 309, 1974.Google Scholar
  70. 70.
    Symoens, J., The Effects of Levamisole on Host Defense Mechanisms, Janssen Pharmaceutical Research Laboratories, Beerse, Belgium, 1975.Google Scholar
  71. 71.
    Mitenko, P. A., and Ogilvie, R. I., Rational intravenous doses of theophylline, W Engl. J. Med., 289, 600, 1973.Google Scholar
  72. 72.
    Nagode, L. A., Haussler, M. R., Bayce, 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 (abstract).Google Scholar
  73. 73.
    Fawaz, E. N., and Tejirian, A., Inhibition of alkaline phosphatase by theophylline in vitro, Hoppe-Seyler’s Z. Physiol. Chem., 353, 1779, 1972.Google Scholar
  74. 74.
    Van Belle, H., Kinetics and inhibition of alkaline phosphatases from canine tissues, Biochim. Biophys. Acta, 289, 158, 1972.Google Scholar
  75. 75.
    Bernfeld, P., Berkeley, B. J., and Bieber, R. E., Reversible dissociation of enzymes at high dilutions and their inhibition by polyanions, Arch. Biochem. Biophys., 777, 31, 1965.Google Scholar
  76. 76.
    Henneman, P. H., Rourke, G. M., and Jackson, W. P. U., Depression of serum alkaline phosphatase activity by human serum albumin, J. Biol. Chem., 213, 19, 1955.Google Scholar
  77. 77.
    Foster, R. L., and Bannister, A., Inhibition of alkaline phosphatase activity by serum albumin, Clin. Chem., 22, 1751, 1976.Google Scholar
  78. 78.
    Bakwin, H., and Bodansky, O., Factors influencing the measurement of the phosphatase activity of tissue extracts, J. Biol. Chem., 101, 641, 1933.Google Scholar
  79. 79.
    Aebi, H., Zur Methodik der Nierenphosphatase-Bestimmung, Helv. Chim. Acta, 31, 1761, 1948.Google Scholar
  80. 80.
    Bodansky, A., Notes on the determination of serum inorganic phosphate and serum phosphatase activity, J. Biol. Chem., 120, 167, 1937.Google Scholar
  81. 81.
    Ruppert, F., Über die Beständigkeit der alkalischen Blutphosphatase bei verschiedenen Temper-aturen, Klin. Wochenschr., 30, 184, 1952.Google Scholar
  82. 82.
    Tietz, N. W., and Green, A., An automated procedure for the determination of phosphorus and alkaline phosphatase (Bodansky) in serum, Clin. Chim. Acta, 9, 392, 1964.Google Scholar
  83. 83.
    Massion, C. G., and Frankenfeld, J. K., Alkaline phosphatase Lability in fresh and frozen human serum and lyophilized control material, Gin. Chem., 18, 366, 1972.Google Scholar
  84. 84.
    Wilson, S. S., Guillan, R. A., and Hocker, E. V., Studies of the stability of 18 chemical con-stituents of human serum, Clin. Chem., 18, 1498, 1972.Google Scholar
  85. 85.
    Kelly, M. H., and Hamilton, J. R., A micro-technique for the assay of intestinal alkaline phosphatase Results in normal children and children with celiac disease, Clin. Biochem., 3, 33, 1970.Google Scholar
  86. 86.
    Cornish, C., Studies on human alkaline phosphatase, M.S. thesis, University of Sydney, Sydney, Australia, 1973.Google Scholar
  87. 87.
    Malamy, M. H., and Horecker, B. L., Purification and crystallization of the alkaline phosphatase of Escherichia coli, Biochemistry, 3, 1893, 1964.Google Scholar
  88. 88.
    Nyc, J. F., Kadner, R. J., and Crocken, B. J., A repressible alkaline phosphatase in Neurospora crassa, J. Biol. Chem., 241, 1468, 1966.Google Scholar
  89. 89.
    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.Google Scholar
  90. 90.
    Kaplan, A., and Narahara, A., The determination of serum alkaline phosphatase activity, J. Lab. Gin. Med., 41, 819, 1953.Google Scholar
  91. 91.
    Bowers, G. N., Jr., and McComb, R. B., Measurement of total alkaline phosphatase activity in human serum, Clin. Chem., 21, 1988, 1975.Google Scholar
  92. 92.
    Szasz, G., Increase of alkaline phosphatase activity in commercial reference sera after reconstitution, Scand. J. Clin. Lab. Invest., 29, Suppl. 126, 1972 (abstract 12.7).Google Scholar
  93. 93.
    Hanok, A., and Kuo, J., The stability of a reconstituted serum for the assay of fifteen chemical constituents, Clin. Chem., 14, 58, 1968.Google Scholar
  94. 94.
    Wallach, D. P., and Ko, H., Some properties of an alkaline phosphatase from rat adipose tissue, Can. J. Biochem., 42, 1445, 1964.Google Scholar
  95. 95.
    McCoy, E. E., Park, J., and England, J., A fluorimetric assay and properties of leukocyte alkaline phosphatase, Clin. Chim. Acta, 72, 453, 1965.Google Scholar
  96. 96.
    Zittle, C. A., and Delia Monica, E. S., Effects of borate and other ions on the alkaline phosphatase of bovine milk and intestinal mocosa, Arch. Biochem., 26, 112, 1950.Google Scholar
  97. 97.
    Dorn, G. L., Purification and characterization of phosphatase I from Aspergillus nidulans, J. Biol Chem., 243, 3500, 1968.Google Scholar
  98. 98.
    Connolly, V. J., A known enzyme concentration as a control in the alkaline phosphatase test, J. Lab. Clin. Med., 42, 657, 1953.Google Scholar
  99. 99.
    Lowry, O. H., Roberts, N. R., Wu, M., Hixon, W. S., and Crawford, E. J., The quantitative histochemistry of brain. II. Enzyme measurements, J. Biol Chem., 207, 19, 1954.Google Scholar
  100. 100.
    Warnock, M., Characterization of tissue and serum alkaline phosphatases, Clin. Chim. Acta. 14, 156, 1966.Google Scholar
  101. 101.
    Laessig, R. H., Schwartz, T. H., Indriksons, A., and Miran, D. E., A study of statistical techniques applied to changes during storage of serum specimens for multiphasic screening, Health Lab. Sci., 9, 269, 1972.Google Scholar
  102. 102.
    Williams, G. Z., Harris, E. K., and Widdowson, G. M., Comparison of estimates of long-term analytical variation derived from subject samples and control serum, Clin. Chem., 23, 100, 1977.Google Scholar
  103. 103.
    Brojer, B., and Moss, D. W., Changes in the alkaline phosphatase activity of serum samples after thawing and after reconstitution from the lyophilized state, Clin. Chim. Acta, 35, 511, 1971.Google Scholar
  104. 104.
    Schneider, A. L., Senior Research Scientist, DADE, Miami, Florida, Personal communication, 1975.Google Scholar
  105. 105.
    Landaas, S., Temperature-dependence of alkaline phosphatase activity in reconstituted control sera, Scand. J. Gin. Lab. Invest., 31, 353, 1973.Google Scholar
  106. 106.
    Czarnetzy, E. M., Richeal, R. J., and O’Malley, J. A., Temperature-dependent changes with time in the alkaline phosphatase activity of commercial control serum, Gin. Chem., 76, 521, 1970.Google Scholar
  107. 107.
    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.Google Scholar
  108. 108.
    Bodansky, O., The energy of activation of the hydrolysis of sodium β-glycerophosphate by bone phosphatase at optimal pH, J. Biol Chem., 129, 197, 1939.Google Scholar
  109. 109.
    Scandinavian Society for Clinical Chemistry, Committee on Enzymes, Recommended methods for the determination of four enzymes in blood, Scand. J. Gin. Lab. Invest., 33, 291, 1974.Google Scholar
  110. 110.
    Kadlecová, L., and Stepan, J., Phosphatases. VI. pH dependence of the organ-specific thermostability of alkaline phosphatases in tissue homogenates, Experientia, 28, 1248, 1972.Google Scholar
  111. 111.
    Rej, R., Effects of incubation with Mg2+ on the measurement of alkaline phosphatase activity, Gin. Chem., 23, 1903, 1977.Google Scholar
  112. 112.
    Seligman, A. M., Chauncey, H. H., and Nachlas, M. M., Effect of formalin fixation on the activity of five enzymes of rat liver, Stain Technol., 26, 19, 1951.Google Scholar
  113. 113.
    Tsou, K. C., and Su, H. C. F., A new colorimetric method for the determination of alkaline phosphatase with indoxylphosphate, Anal. Biochem., 11, 54, 1965.Google Scholar
  114. 114.
    Simpson, R. T., Vallee, B. L., and Tait, G. H., Alkaline phosphatase of Escherichia coli Composition, Biochemistry, 7, 4336, 1968.Google Scholar
  115. 115.
    Lazdunski, M., Petitclerc, C., Chapplet, D., and Lazdunski, C., Flip-flop mechanisms in enzymology-A model The alkaline phosphatase of Escherichia coli, Eur. J. Biochem., 20, 124, 1971.Google Scholar
  116. 116.
    Fernley, H. N., and Walker, P. G., Kinetic behaviour of calf-intestinal alkaline phosphatase with 4-methylumbelliferyl phosphate, Biochem. J., 97, 95, 1965.Google Scholar
  117. 117.
    Morin, L. G., Ammonium thymolphthalein monophosphate as a new substrate for alkaline and acid phosphatase determinations in serum, Gin. Giem., 19, 1135, 1973.Google Scholar
  118. 118.
    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.Google Scholar
  119. 119.
    King, E. J., and Nicholson, T. F., The preparation of phenyl phosphoric esters, Biochem. J., 33, 1182, 1939.Google Scholar
  120. 120.
    Bessey, O. A., and Love, R. H., Preparation and measurement of the purity of the phosphatase reagent, disodium p-nitrophenylphosphate,Biol. Chem., 196, 175, 1952.Google Scholar
  121. 121.
    Aschaffenburg, R., Preparation of the phosphatase reagent disodium p-nitrophenylphosphate, Science, 117, 611, 1953.Google Scholar
  122. 122.
    King, E. J., Preparation of phenolphthalein phosphate, J. Pathol Bacteriol., 55, 311, 1943.Google Scholar
  123. 123.
    Neumann, H., Some new substrates for determinations of phosphatase, Experientia, 4, 74, 1948.Google Scholar
  124. 124.
    Hofstee, B. H. J., Direct and continuous spectrophotometry assay of phosphomonoesterases, Arch. Biochem. Biophys., 51, 139, 1954.Google Scholar
  125. 125.
    Burstone, M. S., Histochemical comparison of naphthol vs. AS-phosphates for the demonstra-tion of phosphatases, J. Natl. Cancer Inst., 20, 601, 1958.Google Scholar
  126. 126.
    Akerfeldt, S., Preparation and determination of sodium-hydrogen 5-(2-aminoethyl) phosphoro-thioate (sodium-hydrogen cysteamine-S-phosphate), Acta Chem. Scand., 13, 1479, 1959.Google Scholar
  127. 127.
    Nielsen, M. L., Ferguson, R. R., and Coakley, W. S., Sodium imidodiphosphate Synthesis, iden-tification and hydrolytic degradation, J. Am. Chem. Soc., 83, 99, 1961.Google Scholar
  128. 128.
    Mitchell, H. K., and Lunan, K. D., Tyrosine-O-phosphate in Drosophila, Arch. Biochem. Bio-phys., 106, 219, 1964.Google Scholar
  129. 129.
    Kirby, A. J., and Varvoglis, A. G., 2,4-Dinitrophenyl phosphate, J. Am. Chem. Soc., 88, 1823, 1966.Google Scholar
  130. 130.
    Coleman, C. M., The synthesis of thymolphthalein monophosphate, a new substrate for alkaline phosphatase, Gin. Chim. Acta, 13, 401, 1966.Google Scholar
  131. 131.
    Horwitz, J. P., Chua, J., Noel, M., Donatti, J. T., and Freisler, J., Substrates for cytochemical demonstration of enzyme activity. II. Some dihalo-3-indolyl phosphates and sulfates, J. Med. Chem., 9, 447, 1966.Google Scholar
  132. 132.
    Kirby, A. J., and Varvoglis, A. G., The reactivity of phosphate esters Monoester hydrolysis, Am. Chem. Soc., 89, 415, 1967.Google Scholar
  133. 133.
    Breslow, R., and Katz, I., Relative reactivities of p-nitrophenyl phosphate and phosphorothioate toward alkaline phosphatase and in aqueous hydrolysis, J. Am. Chem. Soc., 90, 7376, 1968.Google Scholar
  134. 134.
    Mushak, P., and Coleman, J., Hydrolysis of a stable oxygen ester of phosphorothioic acid by alkaline phosphatase, Biochemistry, 11, 201, 1972.Google Scholar
  135. 135.
    Snyder, S. L., and Wilson, I. B., Phosphoramidic acids A new class of nonspecific substrates for alkaline phosphatase from Escherichia coli, Biochemistry, 11, 1616, 1972.Google Scholar
  136. 136.
    Williams, A., Naylor, R. A., and Collyer, S. G., Bacterial alkaline phosphatase. III. Kinetic studies with substituted phenyl phosphates and structurally related inhibitors, J. Chem. Soc. Perkin Trans. 2, 25, 1973.Google Scholar
  137. 137.
    Chlebowski, J. F., and Coleman, J. E., Mechanisms of hydrolysis of O-phosphorothioates and inorganic thiophosphate by Escherichia coli alkaline phosphatase, J. Biol. Chem., 249, 7192, 1974.Google Scholar
  138. 138.
    Salomon, L. L., James, J., and Weaver, P. R., Assay of phosphatase activity by direct spectrophotometry determination of phenolate ion, Anal. Chem., 36, 1162, 1964.Google Scholar
  139. 139.
    Woodin, A. M., Inhibition of the p-nitrophenyl phosphatase of leukocyte membranes by p- nitrophenyl phosphate preparations, Anal. Biochem., 63, 452, 1975.Google Scholar
  140. 140.
    Bowers, G. N., Jr., McComb, R. B., and Horder, M., Reagent quality, a prerequisite for meaningful measurements in clinical enzymology, in Organisation des Laboratoires et Interprétation des Résultats (Siest, G., éd.), p. 257, Expansion Scientifique Française, Paris, 1976.Google Scholar
  141. 141.
    Hill, H. D., Summer, G. K., and Waters, M. D., An automated fluorometric assay for alkaline phosphatase using 3-O-methylfluorescein phosphate, Anal Biochem., 24, 9, 1968.Google Scholar
  142. 142.
    Henningson, R. W., Chemical stability of disodium phenyl phosphate in carbonate-bicarbonate buffer, J. Dairy Sci., 43, 769, 1960.Google Scholar
  143. 143.
    Kirby, A. J., and Jencks, W. P., The reactivity of nucleophilic reagents toward p-nitrophenyl phosphate dianion, J. Am. Chem. Sci., 87, 3209, 1965.Google Scholar
  144. 144.
    Kind, P. R. N., and King, E. J., Estimation of plasma phosphatase by determination of hydrolysed phenol with amino-antipyrine, J. Clin. Pathol., 7, 322, 1954.Google Scholar
  145. 145.
    Fischer, W., and Müller, E., Aktivitätsbestimmung der alkalischen Phosphatase mit Naphthol-AS BS-phosphate als Substrat, Acta Histochem., 40, 1, 1971.Google Scholar
  146. 146.
    Fischl, J., Segal, S., and Rabiah, S., Microdetermination of phosphatase employing Phenolphthalein diphosphate as substrate, Clin. Chem., 13, 941, 1967.Google Scholar
  147. 147.
    Dalai, F. R., and Winsten, S., Thymol blue monophosphate-A new substrate for kinetic alkaline phosphatase determinations, Clin. Chem., 21, 969, 1975.Google Scholar
  148. 148.
    Elser, R. C., Serum alkaline phosphatase measured by using thymol blue monophosphate and a bichromatic analyzer, Clin. Chem., 22, 1737, 1976.Google Scholar
  149. 149.
    Engström, L., Studies on calf-intestinal alkaline phosphatase, Biochim. Biophys. Acta, 52, 36, 1961.Google Scholar
  150. 150.
    Moss, D. W., A note on the spectrophotometry estimation of alkaline phosphatase activity, Enzymologia, 31, 193, 1966.Google Scholar
  151. 151.
    Stevens, J., and Thomas, F., Alkaline phosphatase Reaction rate analysis at 340 nm, Clin. Chim. Acta, 37, 541, 1972.Google Scholar
  152. 152.
    Harper, R. A., and Armstrong, F. B., Alkaline phosphatase of Drosophila melanogaster. III. Tyrosine-O-phosphate as substrate, Biochem. Genet., 11, 111, 1974.Google Scholar
  153. 153.
    Bowers, G. N., Jr., Kelley, M. L., and McComb, R. B., Continuous spectrophotometry measurement of serum alkaline phosphatase activity Relative molecular activity and sensitivity of nine self-indicating phenolic substrates in 2-amino-2-methyl-l-propanol buffer, Clin. Chem., 13, 608, 1967.Google Scholar
  154. 154.
    Fischer, F., and Siebert, G., Optischer Test zur Bestimmung der alkalischen Phosphatase im Serum, Klin. Wochenschr., 39, 202, 1961.Google Scholar
  155. 155.
    Sanadi, D. R., Enzymatic dephosphorylation of triphosphopyridine nucleotide, Arch. Biochem., 35, 268, 1952.Google Scholar
  156. 156.
    Pitkanen, E., The hydrolysis of nicotinamide adenine dinucleotide phosphate by serum alkaline phosphatase, Enzyme, 12, 266, 1971.Google Scholar
  157. 157.
    Harkness, D. R., Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme, Arch. Biochem. Biophys., 126, 513, 1968.Google Scholar
  158. 158.
    Weissman, N., and Pileggi, V. J., Inorganic ions, in Clinical Chemistry, Principles and Technics, 2nd ed. (Henry, R. J., Cannon, D. C., and Winkelman, J. W., eds.), p. 720, Harper and Row, Hagerstown, Maryland, 1974.Google Scholar
  159. 159.
    Klein, B., Read, P. A., and Babson, A. L., Rapid method for the quantitative determination of serum alkaline phosphatase, Clin. Chem., 6, 269, 1960.Google Scholar
  160. 160.
    Borst Pauwels, G. W. F. H., Occurrence of Phenolphthalein monophosphate as an intermediate in the enzymatic hydrolysis of Phenolphthalein diphosphate to Phenolphthalein and orthophosphate, Nature (London), 202, 190, 1964.Google Scholar
  161. 161.
    Kaplow, L. S., A histochemical procedure for localizing and evaluating leukocyte alkaline phosphatase activity in smears of blood and marrow, Blood, 10, 1023, 1955.Google Scholar
  162. 162.
    Taswell, H. F., and Jeffers, D. M., Isoenzymes of serum alkaline phosphatase in hepatobiliary and skeletal diseases, Am. J. Clin. Pathol., 40, 349, 1963.Google Scholar
  163. 163.
    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.Google Scholar
  164. 164.
    Lee, L. M. Y., and Kenny, M. A., Electrophoretic method for assessing the normal and pathological distribution of alkaline phosphatase isoenzymes in serum, Clin. Chem., 21, 1128, 1975.Google Scholar
  165. 165.
    Kaplow, L. S., Leukocyte alkaline phosphatase in disease, in CRC Critical Reviews in Clinical Laboratory Sciences, Vol. 2 (King, J. W., and Faulkner, W. R., eds.), p. 243, CRC Press, Cleveland, Ohio, 1971.Google Scholar
  166. 166.
    Fritsche, H. A., Jr., and Adams-Park, H. R., Cellulose acetate electrophoresis of alkaline phosphates isoenzymes in human serum and tissue, Clin. Chem., 18, 417, 1972.Google Scholar
  167. 167.
    Epstein, E., Wolf, P. I., Horwitz, J. P., and Zak, B., An indigogenic reaction for alkaline phosphatase in disc electrophoresis, A m. J. Clin. Pathol., 48, 530, 1967.Google Scholar
  168. 168.
    McGadey, J., A tetrazolium method for non-specific alkaline phosphatase, Histochemie, 23, 180, 1970.Google Scholar
  169. 169.
    Kezdy, F., and Bender, M. J., The kinetics of the a-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetat Q, Biochemistry, 1, 1097, 1962.Google Scholar
  170. 170.
    Richterich, R., and Gautier, E., Ultramikromethoden im klinischen Laboratorium. IV. Bestim-mung der alkalischen Serumphosphatase, Schweiz. Med. Wochens ehr., 92, 781, 1962.Google Scholar
  171. 171.
    German Society for Clinical Chemistry, Standard method for determination of alkaline phosphatase (AP) activity, Z. Klin. Chem. Klin. Biochem., 10, 290, 1972.Google Scholar
  172. 172.
    Reid, T. W., and Wilson, I. B., Conformational isomers of alkaline phosphatases in the mechanism of hydrolysis, Biochemistry, 10, 380, 1971.Google Scholar
  173. 173.
    Axelrod, B., A Study of the mechanism of “phosphotransferase” activity by use of radioactive phosphorus, J. Biol. Chem., 176, 295, 1948.Google Scholar
  174. 174.
    Engström, L., Formation of a phosphorylenzyme during hydrolysis of 32P-labelled glucose 6- phosphate by alkaline phosphatase from calf-intestinal mucosa and Escherichia coli, Ark. Kemi, 19, 129, 1962.Google Scholar
  175. 175.
    Aw, S. E., The radiometric assay of alkaline phosphatase activity with 125I-labelled Phenolphthalein monophosphate, Clin. Chim. Acta, 60, 315, 1975.Google Scholar
  176. 176.
    Dalgaard, J. B., Tracer phosphatase determination in tissue sections, Nature (London), 162, 811, 1948.Google Scholar
  177. 177.
    Barnard, P. W. C., Bunton, C. A., Kellerman, D., Mhala, M. M., Silver, B., Vernon, C. A., and Welch, V. A., Reactions of organic phosphates. Part VI. The hydrolysis of aryl phosphates, J. Chem. Soc. B, 227, 1966.Google Scholar
  178. 178.
    Proksch, G. J., Preparation of sodium thymolphthalein monophosphate, an economical sub-strate for measurement of alkaline and acid phosphatase activities, Clin. Chem., 18, 93, 1972.Google Scholar
  179. 179.
    Bergmeyer, H. U., Determination of enzyme activities, in Principles of Enzymatic Analysis (Bergmeyer, H. U., ed.), 2nd English ed., Vol. 1, p. 129, Verlag Chemie, Weinheim, 1974.Google Scholar
  180. 180.
    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.Google Scholar
  181. 181.
    Van Belle, H., Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified iso-enzymes from humans, Clin. Chem., 22, 972, 1976.Google Scholar
  182. 182.
    Van Belle, H., Alkaline Phosphatase. II. Conditions affecting determination of total activity in serum, Clin. Chem., 22, 977, 1976.Google Scholar
  183. 183.
    Skillen, A. W., and Harrison, J., Serum alkaline phosphatases-Effect of pH and buffer on optimum substrate concentration, Clin. Chim. Acta, 45, 287, 1973.Google Scholar
  184. 184.
    Williams, A., and Naylor, R. A., Evidence for Sn2(P) mechanism in the phosphorylation of alkaline phosphatase by substrates,J. Chem. Soc. B, 1973, 1971.Google Scholar
  185. 185.
    Ross, M. H., Ely, J. O., and Archer, J. G., Alkaline phosphatase and pH optima, J. Biol. Chem., 192, 561, 1951.Google Scholar
  186. 186.
    Cathala, G., Brunei, 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.Google Scholar
  187. 187.
    Schwartz, M. K., Kessler, G., and Bodansky, O., Comparison of serum alkaline phosphatase activities determined with sodium β-glycerophosphate and sodium phenylphosphate as substrates, Am. J. Clin. Pathol., 33, 275, 1960.Google Scholar
  188. 188.
    Bretaudière, J.-P., Amsellem, L., Dumont, G., Pourci, M.-L., Phung, H.-T., Vassault, A., and Bailly, M., Mise au point d’une méthode standardisée a 30°C pour la determination de l’activité catalytique de la phosphatase alcaline, in Organisation des Laboratories et Interprétation des Résults (Siest, G., ed.), p. 287, Expansion Scientifique Française, Paris, 1976.Google Scholar
  189. 188a.
    Bretaudière, J.-P., Vassault, A., Amsellem, L., Pourci, M.-L., Thieu-Phung, H., and Bailly, M., Criteria for establishing a standard method for determining alkaline phosphatase activity in human serum, Clin. Chem., 23, 2263, 1977.Google Scholar
  190. 189.
    Schmidt, G., and Thannhauser, S. J., Intestinal phosphatase, J. Biol. Chem., 149, 369, 1943.Google Scholar
  191. 190.
    Stolbach, L. L., Nisselbaum, J. S., and Fishman, W. H., A simplified technic for measuring serum acid phosphatase of prostatic origin (Fishman-Lerner method), Am. J. Clin. Pathol., 29, 379, 1958.Google Scholar
  192. 191.
    Deren, J. J., Williams, L. A., Muench, H., Chalmers, T., and Zamcheck, N., Comparative study of four methods of determining alkaline phosphatase, N. Engl. J. Med., 270, 1277, 1964.Google Scholar
  193. 192.
    Fonty, P. P., Leduc, C., and Vernin, H., Etude comparative de quelques méthodes de dosage des phosphatases (alcaline et acide) choix d’une méthode, Ann. Biol. Clin., 20, 617, 1962.Google Scholar
  194. 193.
    Gelb, D., West, M., and Zimmerman, H. J., The relation of the Bodansky to the King-Armstrong method for the determination of the serum alkaline phosphatase, Am. J. Clin. Pathol., 38, 198, 1962.Google Scholar
  195. 194.
    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.Google Scholar
  196. 195.
    Nisselbaum, J. S., Schlamowitz, M., and Bodansky, O., Immunochemical studies of functionally similar enzymes, Ann. N. Y. Acad. Sci., 94, 970, 1961.Google Scholar
  197. 196.
    Behal, F. J., and Center, M., Heterogeneity of calf intestinal alkaline phosphatase, Arch. Biochem. Biophys., 110, 500, 1965.Google Scholar
  198. 197.
    Etzler, M. E., and Moog, F., Immunochemical characterization of alkaline phosphatase isoenzymes of the young mouse duodenum, Biochim. Biophys. Acta, 154, 150, 1968.Google Scholar
  199. 198.
    Wolf, M., Dinwoodie, A., and Morgan, H. G., Comparison of alkaline phosphatase isoenzymes activity using five standard methods, Clin. Chim. Acta, 24, 131, 1969.Google Scholar
  200. 199.
    Folley, S. J., and Kay, H. D., The alkaline Phosphomonoesterase of the mammary gland, Biochem. J., 29, 1837, 1935.Google Scholar
  201. 200.
    King, E. J., and Delory, G. E., The rates of enzymatic hydrolysis of phosphoric esters, Biochem. J., 33, 1185, 1939.Google Scholar
  202. 201.
    Neumann, H., Dependence of the pH-optimum of the Phosphomonoesterase on the substrate concentration and on inhibitors and activators, Biochim. Biophys. Acta, 3, 117, 1949.Google Scholar
  203. 202.
    Morton, R. K., The kinetics of hydrolysis of phenyl phosphate by alkaline phosphatases, Biochem. J., 65, 674, 1957.Google Scholar
  204. 203.
    Motzok, I., and Branion, H. D., Studies on alkaline phosphatase. 2. Factors influencing pH optima and Michaelis constant, Biochem. J., 72, 111, 1959.Google Scholar
  205. 204.
    Delory, G. E., and King, E. J., The rate of enzymic hydrolysis of phosphoric esters. 2. Relation of structure to dissociation constant, Michaelis constant and rate of hydrolysis, Biochem. J., 37, 547, 1943.Google Scholar
  206. 205.
    Walker, P. G., and King, E. J., The rate of enzymic hydrolysis of phosphoric esters, Biochem. J., 47, 93, 1950.Google Scholar
  207. 206.
    Morton, R. K., The substrate specificity and inhibition of alkaline phosphatases of cow’s milk and calf intestinal mucosa, Biochem. J., 61, 232, 1955.Google Scholar
  208. 207.
    Motzok, I., Studies on alkaline phosphatases. 1. Kinetics of plasma phosphatase of normal and rachitic chicks, Biochem. J., 72, 169, 1959.Google Scholar
  209. 208.
    Aebi, H., and Abelin, I., Die Wirkungsweise verschiedener Effektoren auf die Aktivität der alkalischen Nierenphosphatase (Magnesium, Mangan, Na-Carbonat-Hydrogencarbonat, Ammonium- Ionen und Aminosäuren), Helv. Chim. Acta, 31, 1943, 1948.Google Scholar
  210. 209.
    Morton, R. K., Some properties of alkaline phosphatase of cow’s milk and calf intestinal mucosa, Biochem. J., 60, 573, 1955.Google Scholar
  211. 210.
    Bodansky, O., The accelerant effect of a-amino acids on the activity of bone phosphatase, J. Biol. Chem., 114, 273, 1936.Google Scholar
  212. 211.
    Bodansky, O., The effect of a-amino acids and magnesium on the activity of kidney and intestinal phosphatases, J. Biol. Chem., 115, 101, 1936.Google Scholar
  213. 212.
    Albert, A., Quantitative studies of the avidity of naturally occurring substances for trace metals. I. Aminoacids having only two ionizing groups, Biochem. J., 47, 531, 1950.Google Scholar
  214. 213.
    Perkins, D. J., A study of the amino-acid complexes formed by metals of group II of the peri-odic classification, Biochem. J., 51, 487, 1952.Google Scholar
  215. 214.
    Fisher, J. F., and Hall, J. L., A polorographic study of the copper (II) complexes of mono-, di-, and triethanolamine, Anal. Chem., 34, 1094, 1962.Google Scholar
  216. 215.
    Allen, D. E., Baker, D. J., and Gillard, R. D., Metal complexing by Tris buffer, Nature (London), 214, 906, 1967.Google Scholar
  217. 216.
    King, E. S., Haslewood, G. A. D., and Delory, G. E., Micro-chemical methods of blood analysis, Lancet, 1, 886, 1937.Google Scholar
  218. 217.
    King, E. J., Haslewood, G. A. D., Delory, G. E., and Beall, D., Micro-chemical methods of blood analysis, Lancet, 1, 207, 1942.Google Scholar
  219. 218.
    King, E. J., Abul-Fadl, M. A. M., and Walker, P. G., King-Arm strong phosphatase estimation by the determination of liberated phosphate, J. Clin. Pathol., 85, 1951.Google Scholar
  220. 219.
    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.Google Scholar
  221. 220.
    Delory, G. E., and King, E. J., A sodium carbonate-bicarbonate buffer for alkaline phosphatases, Biochem. J., 39, 245, 1945.Google Scholar
  222. 221.
    Bates, R. G., Determination of pH Theory and Practice, 2nd ed., Chapt. 4, Wiley & Sons, New York, 1973.Google Scholar
  223. 222.
    Moss, D. W., Baron, D. N., Walker, P. G., and Wilkinson, J. H., Standardization of clinical en-zyme assays, J. Clin. Pathol., 24, 740, 1971.Google Scholar
  224. 223.
    Whitaker, K. B., and Moss, D. W., A comparison of the transphosphorylating activities of human liver and intestinal alkaline phosphatase, Clin. Chim. Acta, 52, 347, 1974.Google Scholar
  225. 224.
    Kadner, R. J., Nyc, J. F., and Brown, D. M., A repressible alkaline phosphatase in Neurospora crassa, J. Biol. Chem., 243, 3076, 1968.Google Scholar
  226. 225.
    Hofstee, B. H. J., Alkaline phosphatase. I. Mechanism of action of Zn, Mg, glycine, versene and hydrogen ions, Arch. Biochem. Biophys., 59, 352, 1955.Google Scholar
  227. 226.
    Bodansky, O., Mechanism of inhibition of phosphatase activity by glycine, J. Biol. Chem., 165, 605, 1946.Google Scholar
  228. 227.
    Haije, W. G., Influence of buffer conditions on the activities of some iso-enzymes of alkaline phosphatase in the serum, Clin. Chim. Acta, 48, 23, 1973.Google Scholar
  229. 228.
    MacWilliam, K. M., Moody, A. H., and Silk, J., Variation in alkaline phosphatase results using the method of Bessey, Lowry and Brock, Clin. Chim. Acta, 17, 514, 1967.Google Scholar
  230. 229.
    Gomori, G., Buffers in the range of pH 6.5 to 9.6, Proc. Soc. Exp. Biol Med., 62, 33, 1946.Google Scholar
  231. 230.
    Granger, R., and Fraux, J., Aminocyclanols et phosphomonoesterase alcaline, Trav. Soc. Pharm. Montpellier, 7, 22, 1947.Google Scholar
  232. 231.
    Zittle, C. A., and Delia Monica, E. S., Effects of glutamic acid, lysine, and certain inorganic ions on bovine alkaline phosphatases, Arch. Biochem., 26, 135, 1950.Google Scholar
  233. 232.
    Mathies, J. C., Preparation and properties of highly purified alkaline phosphatase from swine kidneys, J. Biol Chem., 233, 1121, 1958.Google Scholar
  234. 233.
    Amador, E., and Urban, J., Transphosphorylation by human alkaline phosphatases, Am. J. Clin. Pathol., 57, 167, 1972.Google Scholar
  235. 234.
    Fleisher, G. A., Eickelberg, E. S., and Elveback, L. R., Alkaline phosphatase activity in the plasma of children and adolescents, Clin. Chem., 23, 469, 1977.Google Scholar
  236. 235.
    Bloch, W., and Schlesinger, M. J., Kinetics of substrate hydrolysis by molecular variants of Escherichia coli alkaline phosphatase, J. Biol Chem., 249, 1760, 1974.Google Scholar
  237. 236.
    Durst, R. A., and Staples, B. R., Tris/Tris • HC1 A standard buffer for use in the physiologic pH range, Clin. Chem., 18, 206, 1972.Google Scholar
  238. 237.
    Amador, E., and Wacker, W. E. C., Enzymatic methods used for diagnosis, in Methods of Biochemical Analysis, Vol. 13 (Glick, D., ed.), p. 265, Interscience, New York, 1965.Google Scholar
  239. 238.
    Kleyn, D. H., Utilization of phenolphthalein monophosphate to determine the phosphatase activity of milk, J. Milk Food Technol., 35, 405, 1972.Google Scholar
  240. 239.
    Herz, F., and Sevdalian, D. A., Regulation of alkaline phosphatase activity in human cell cultures Role of serum, Arch. Biochem. Biophys., 146, 1, 1971.Google Scholar
  241. 240.
    Ohkubo, A., Langerman, N., and Kaplan, M. M., Rat liver alkaline phosphatase Purification and properties, J. Biol Chem., 249, 7174, 1974.Google Scholar
  242. 241.
    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
  243. 242.
    Walter, K., and Schutt, C., Alkaline phosphatase in serum (continuous assay), in Methods of Enzymatic Analysis (Bergmeyer, H. U., ed.), 2nd ed. (English ed.), p. 860, Academic Press, New York, 1974.Google Scholar
  244. 243.
    Zech, R., Grote, M., Ziircher, K., and Schlaeger, R., Uber die Phosphorylierung von Diathanola-min durch alkalische Phosphatase, Z. Klin. Chem. Klin. Biochem., 11, 461, 1973.Google Scholar
  245. 244.
    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.Google Scholar
  246. 245.
    Simpson, E., McAllister, E. J., and Hainsworth, I. R., The quality control of alkaline phosphatase determinations with placental phosphatase, Clin. Chim. Acta, 77, 415, 1977.Google Scholar
  247. 246.
    LeHégarat, 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
  248. 247.
    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.Google Scholar
  249. 248.
    Glew, R. H., and Heath, E. C., Studies on the extracellular alkaline phosphatase of Micrococcus sodonensis. I. Isolation and characterization, J. Biol. Chem., 246, 1556, 1971.Google Scholar
  250. 249.
    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.Google Scholar
  251. 250.
    Frank, J. J., Bermes, E. W., Bickel, M. J., and Watkins, B. F., Effect of in vitro hemolysis on chemical values for serum, Clin. Chem., 24, 1966, 1978.Google Scholar
  252. 251.
    Szasz, G., Effect of ions on the alkaline phosphatase activity, Clin. Chem., 19,664,1973 (Abstr. No. 134).Google Scholar
  253. 252.
    Ahmed, Z., Abul-Fadl, M. A. M., and King, E. J., The co-enzyme factor of alkaline phosphatase, Biochim. Biophys. Acta, 36, 228, 1959.Google Scholar
  254. 253.
    Fernley, H. N., and Walker, P. G., Studies on alkaline phosphatase Inhibition by phosphate derivatives and the substrate specificity, Biochem. J., 104, 1011, 1967.Google Scholar
  255. 254.
    Posen, S., Cornish, C. J., Home, M., and Saini, P. K., Placental alkaline phosphatase and pregnancy, Ann. N. Y. Acad. Sci., 166, 733, 1969.Google Scholar
  256. 255.
    Cloetens, R., Reversible Abspaltung des zweiten Metalles der alkalischen Phosphatase II, Biochem. Z., 308, 37, 1941.Google Scholar
  257. 256.
    Bowers, G. N., Jr., McComb, R. B., and Kelley, M. L., Effect of magnesium on alkaline phosphatase activity in human serum, Clin. Chem., 23, 1149, 1977 (abstract).Google Scholar
  258. 257.
    Roy, A. V., Rapid method for determining alkaline phosphatase activity in serum with thy-molphthalein monophosphate, Clin. Chem., 76, 431, 1970.Google Scholar
  259. 258.
    Jenner, H. D., and Kay, H. D., The phosphatases of mammalian tissues. III. Magnesium and the phosphatase system, J. Biol. Chem., 93, 733, 1931.Google Scholar
  260. 259.
    Davis, F. W. J., and Lees, H., Alkaline phosphatases of Neurospora crassa. I, Can. J. Microbiol, 15, 455, 1969.Google Scholar
  261. 260.
    Bosron, W. F., Anderson, R. A., Falk, M. C., Kennedy, F. S., and Vallee, B. L., Effect of mag-nesium on the properties of zinc alkaline phosphatase, Biochemistry, 16, 610, 1977.Google Scholar
  262. 261.
    Coutinho, H. B., Katchburian, E., and Pearse, A. G. E., Effects of Triton-X-100 upon the mobility of esterases and alkaline phosphatases in disc electrophoresis, J. Clin. Pathol, 19, 617, 1966.Google Scholar
  263. 262.
    Mather, I. H., and Keenan, T. W., The stability of alkaline phosphatase in sodium dodecyl sulfate, FEBS Lett., 44, 79, 1974.Google Scholar
  264. 263.
    Fishman, L., Acrylamide disc gel electrophoresis of alkaline phosphatase of human tissues, serum and ascites fluid using Triton X-100 in the sample and the gel matrix, Biochem. Med., 309, 1974.Google Scholar
  265. 264.
    Winsted, M., Reagent Grade Water How, When, Why, pp. 19 and 109, American Society of Medical Technologists, Austin, Texas, 1967.Google Scholar
  266. 265.
    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
  267. 266.
    Home, M., Cornish, C. J., and Posen, S., The use of urea denaturation in the identification of human alkaline phosphatases,JLab. Clin. Med., 72, 905, 1968.Google Scholar
  268. 267.
    Fishman, W. H., Perspectives on alkaline phosphatase isoenzymes, Am. J. Med., 56, 617, 1974.Google Scholar
  269. 268.
    Fishman, W. H., and Green, S., Automated differential isoenzyme analysis. I. L-Phenylalanine- sensitive isoenzymes of human serum alkaline phosphatase, Enzymologia, 33, 89, 1967.Google Scholar
  270. 269.
    Green, S., Anstiss, C. L., and Fishman, W. H., Automated differential isoenzyme analysis. II. The fractionation of serum alkaline phosphatases into “liver,” “intestinal” and “other” components, Enzymologia, 41, 9, 1911.Google Scholar
  271. 270.
    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.Google Scholar
  272. 271.
    Fernley, H. N., and Walker, P. G., Inhibition of alkaline phosphatase by L-phenylalanine, Biochem.J., 116, 543, 1970.Google Scholar
  273. 272.
    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.Google Scholar
  274. 273.
    Ghosh, N. K., Purification and molecular properties of placental and intestinal alkaline phosphatase, Ann. N. Y. Acad. Sci., 166, 604, 1969.Google Scholar
  275. 274.
    Fishman, W. H., and Sie, H.-G., Organ-specific inhibition of human alkaline phosphatase iso-enzymes of liver, bone, intestine and placenta L-Phenylalanine, L-tryptophan and L-homo- arginine, Enzymologia, 41, 141, 1971.Google Scholar
  276. 275.
    Lee, M. H., Huang, Y.-M., Agrawal, K. C., and Sartorelli, A. C., Inhibitors of alkaline phos-phatase of sarcoma 180JTG,Biochem. Pharmacol., 24, 1175, 1975.Google Scholar
  277. 276.
    Albers, H., Beyer, E., Bohnenkamp, A., and Müller, G., Über die zusammengesetzte Natur der Fermente, I. Mitteil, (zugleich VI. Mitteil.) zur Kenntnis der Phosphatasen, Chem. Ber., 71, 1913, 1938.Google Scholar
  278. 277.
    Kumai, S., Uber die Phosphomonoesterase, J. Biochem. (Tokyo), 33, 277, 1941.Google Scholar
  279. 278.
    Thoai, N.-V., Roche, J., and Roger, M., Inactivation et réactivation complètes de la phospho- monoestérase alcaline et interchangeabilité des métaux actifs, Biochim. Biophys. Acta, 7, 61, 1947.Google Scholar
  280. 279.
    Abul-Fadl, M. A. M., and King, E. J., Reactivation of alkaline phosphatases after dialysis, Biochem. J., 44, 435, 1949.Google Scholar
  281. 280.
    Ek, B., von Euler, H., and Hahn, L., Zur Kenntnis tierischer Phosphatasen, V., Ark. Kemi, 1, 117. 1949.Google Scholar
  282. 281.
    Kutscher, W., and Sieg, H., Über die Wirkgruppe der Phosphatase, Naturwissenschaften, 37, 451. 1950.Google Scholar
  283. 282.
    Lora-Tamayo, M., and Municio, A. M., Coenzyme of kidney phosphatase, Nature (London), 168, 249, 1951.Google Scholar
  284. 283.
    Akamatsu, S., and Kobayashi, K., Chemical nature of the co-phosphomonoesterase, Enzymologia, 15, 154, 1951.Google Scholar
  285. 284.
    Akamatsu. S., and Aso, Y., Coenzyme of alkaline Phosphomonoesterase, Enzymologia, 16, 231, 1953.Google Scholar
  286. 285.
    Lora-Tamayo, M., and Alvarez, E. F., Coenzyme of kidney phosphatase, Nature (London), 173, 548, 1954.Google Scholar
  287. 286.
    Dixon, M., and Webb, E. C., Enzymes, 2nd ed., Academic Press, New York, 1964.Google Scholar
  288. 287.
    Yeh, M.-F., and Trela, J. M., Purification and characterization of a repressible alkaline phosphatase from Thermus aquaticus, J. Biol. Chem., 251, 3134, 1976.Google Scholar
  289. 288.
    Hulett-Cowling, F. M., and Campbell, L. L., Purification and properties of an alkaline phosphatase of Bacillus licheniformis, Biochemistry, 10, 1364, 1971.Google Scholar
  290. 289.
    Hiwada, K., and Wachsmuth, E. D., Catalytic properties of alkaline phosphatase from pig kidney, Biochem. J., 141, 283, 1974.Google Scholar
  291. 290.
    International Federation of Clinical Chemistry, Expert Panel on Enzymes, Draft Proposal (No. 8) for I.F.C.C. Reference Methods for Enzymes. I. General Considerations Concerning the Standardization of Measurements of Enzyme Activity in Human Serum and Jor Plasma, Clin. Chem., 19, 268, 1973.Google Scholar
  292. 291.
    Mangum, B. W., The gallium melting-point standard Its role in our temperature measurement system, Clin. Chem., 23, 711, 1977.Google Scholar
  293. 292.
    Thornton, D. D., The gallium melting-point standard A determination of the liquid-solid equilibrium temperature of pure gallium on the international practical temperature scale of 1968, Clin. Chem., 23, 719, 1977.Google Scholar
  294. 293.
    Sostman, H. E., The gallium melting-point standard Its role in manufacture and quality control of electronic thermometers for the clinical laboratory, Clin. Chem., 23, 725, 1977.Google Scholar
  295. 294.
    Bowers, G. N., Jr., and Inman, S. R., The gallium melting-point standard Its application and evaluation for temperature measurements in the clinical laboratory, Clin. Chem., 23, 733, 1977.Google Scholar
  296. 295.
    Tiffany, T. O., Thayer, P. C., Coelho, C. M., and Manning, G. B., A propagation of error analysis of the enzyme activity expression A model for determining the total system random error of a kinetic enzyme analyzer, Clin. Chem., 22, 1439, 1976.Google Scholar
  297. 296.
    Maclin, E., Rohlfing, D., and Ansour, M., Relationship between variables in instrument performance and results of kinetic enzyme assays-A system view, Clin. Chem., 79, 832, 1973.Google Scholar
  298. 297.
    Chlebowski, J. F., and Coleman, J. E., Presteady state kinetics of phosphorothioate hydrolysis by alkaline phosphatase Rate-limiting dephosphorylation at alkaline pH, J. Biol. Chem., 247, 6007, 1972.Google Scholar
  299. 298.
    Bowie, L., Esters, F., Bolin, J., and Gochman, N., Development of an aqueous temperature- indicating technique and its application to clinical laboratory instrumentation, Clin. Chem., 22, 449, 1976.Google Scholar
  300. 299.
    Burtis, C. A., Seibert, L. E., Baird, M. A., and Sampson, E. J., Temperature dependence of the absorbance of alkaline solutions of 4-nitrophenylphosphate-A potential source of error in the measurement of alkaline phosphatase, Clin. Chem., 23, 1541, 1977.Google Scholar
  301. 300.
    Gambino, S. R., Temperature for enzyme assays, in Second International Symposium on Clinical Enzymology (Tietz, N. W., Weinstock, A., and Rodgerson, D. E., eds.), p. 311, American Association of Clinical Chemists, Washington, D.C., 1976.Google Scholar
  302. 301.
    Bodansky, A., Determination of serum inorganic phosphate and serum phosphatase, Am. J. Clin. Pathol., Tech. Suppl., 7, 51, 1937.Google Scholar
  303. 302.
    Jenkins, W. T., and D’Ari, L., The kinetics of alkaline phosphatase, J. Biol Chem., 241, 295, 1966.Google Scholar
  304. 303.
    Atwood, J. G., and DiCesare, J. L., Making enzymatic methods optimum for measuring compounds with a kinetic analyzer, Clin. Chem., 21, 1263, 1975.Google Scholar
  305. 304.
    Gibson, Q. H., and Milnes, L., Apparatus for rapid and sensitive spectrophotometry, Biochem. J., 91, 161, 1964.Google Scholar
  306. 305.
    Fernley, H. N., and Bisaz, S., Studies on alkaline phosphatase Phosphorylation of calf-intestinal alkaline phosphatase by 32P-labelled pyrophosphate, Biochem. J., 107, 279, 1968.Google Scholar
  307. 306.
    Manning, J. P., Steinetz, B. G., Babson, A. L., and Butler, M. C., A simple and reliable method for estimation of alkaline phosphatase in tissue homogenates, Enzymologia, 31, 309, 1966.Google Scholar
  308. 307.
    Tiffany, T. O., Watsky, M. B., Burtis, C. A., and Thacker, L. H., Fluorometric fast analyzer Some applications to fluorescence measurements in clinical chemistry, Clin. Chem., 19, 871, 1973.Google Scholar
  309. 308.
    Demetriou, J. A., Drewes, P. A., and Gin, J. B., Enzymes, in Clinical Chemistry, 2nd ed. (Henry, R. J,, Cannon, D. C., and Winkelman, J. W., eds.), p. 929, Harper & Row, Hagerstown, Maryland, 1974.Google Scholar
  310. 309.
    Newfield, O. E., Anomalies in the automated method for determining serum alkaline phosphatase content,Med. J. Aust., 7, 545, 1968.Google Scholar
  311. 310.
    Bell, J. L., Collier, M., and Hartmann, A. M., A shortened automated procedure for the determination of alkaline phosphatase, J. Clin. Pathol, 7 7, 301, 1964.Google Scholar
  312. 311.
    Sterling, R. E., Wilcox, A. A., Ware, A. G., and Umehara, M. K., An automated determination of alkaline phosphatase utilizing p-nitrophenol phosphate, Clin. Chem., 10, 1112, 1964.Google Scholar
  313. 312.
    Hviid, K., An automated alkaline phosphatase assay with phenolphthalein monophosphate as substrate, Clin. Chem., 13, 281, 1967.Google Scholar
  314. 313.
    Klein, B., and Kaufman, J. H., Automated alkaline phosphatase determination. III. Evaluation of phenolphthalein monophosphate, Clin. Chem., 13, 290, 1967.Google Scholar
  315. 314.
    Moss, D. W., The relative merits and applicability of kinetic and fixed-incubation methods of enzyme assay in clinical enzymology, Clin. Chem., 18, 1449, 1972.Google Scholar
  316. 315.
    Powell, M. E. A., and Smith, M. J. H., The determination of serum acid and alkaline phosphatase activity with 4-aminoantipyrine (AAP), J. Clin. Pathol, 7, 245, 1954.Google Scholar
  317. 316.
    Fiske, C. H., and Subbarow, Y., The colorimetric determination of phosphorus, J. Biol Chem., 66, 375, 1925.Google Scholar
  318. 317.
    Dryer, R. L., Tammes, A. R., and Routh, J. I., The determination of phosphorus and phos-phatase with N-phenyl-p-phenylenediamine, J. Biol Chem., 225, 111, 1957.Google Scholar
  319. 318.
    Marsh, B. B., The estimation of inorganic phosphate in the presence of adenosine triphosphate, Biochim. Biophys. Acta, 32, 357, 1959.Google Scholar
  320. 319.
    Robinson, R., Roughan, M. E., and Wagstaff, D. F., Measuring inorganic phosphate without using a reducing agent, Ann. Clin. Biochem., 8 (Pt. 5), 168, 1971.Google Scholar
  321. 320.
    Akamatsu, S., Some micromethods for enzyme studies, J. Biochem. (Tokyo), 39, 203, 1952.Google Scholar
  322. 321.
    Itaya, K., and Ui, M., A new micromethod for the colorimetrie determination of inorganic phosphate, Clin. Chim. Acta, 14, 361, 1966.Google Scholar
  323. 322.
    Eibl, H., and Lands, W. E. M., A new, sensitive determination of phosphate, Anal. Biochem., 30, 51, 1969.Google Scholar
  324. 323.
    Wattiaux, R., and deDuve, C., Tissue fractionation studies. 7. Release of bound hydrolases by means of Triton X-100, Biochem. J., 63, 606, 1956.Google Scholar
  325. 324.
    See, Y. P., and Fitt, P. S., Determination of inorganic phosphate in the presence of Triton X-100, Anal. Biochem., 49, 430, 1972.Google Scholar
  326. 325.
    Tashima, Y., Removal of protein interference in the Fiske Subbarow method by sodium dodecyl sulfate, Anal. Biochem., 69, 410, 1975.Google Scholar
  327. 326.
    El-Dorry, H. F. A., Medina, H., and Bacila, M., Interference of phenothiazine compounds in the colorimetrie determination of inorganic phosphate, Anal. Biochem., 47, 329, 1972.Google Scholar
  328. 327.
    Harder, M., Colorimetrie determination of orthophosphate in the assay of inorganic pyrophos-phatase activity, Anal. Biochem49, 37, 1972.Google Scholar
  329. 328.
    King, E. J., and Delory, G. E., Ascorbic acid and phosphatase activity, Biochem. J., 32, 1157, 1938.Google Scholar
  330. 329.
    Weil-Malherbe, H., and Green, R. H., The catalytic effect of molybdate on the hydrolysis of organic phosphate bonds, Biochem. J., 49, 286, 1951.Google Scholar
  331. 330.
    Lowry, O. H., and Lopez, J. A., The determination of inorganic phosphate in the presence of labile phosphate esters, J. Biol. Chem., 162, 421, 1946.Google Scholar
  332. 331.
    Baginski, E. S., Foa, P. P., and Zak, B., Determination of phosphate Study of labile organic phosphate interference, Clin. Chim. Acta, 15, 155, 1967.Google Scholar
  333. 332.
    Harder, M., Inorganic pyrophosphatase activity in human sera with elevated alkaline ortho–phosphatase activity, Clin. Chim. Acta, 42, 373, 1972.Google Scholar
  334. 333.
    Skeggs, L. T., Jr., An automatic method for colorimetrie analysis, Am. J. Clin. Pathol., 28, 311, 1957.Google Scholar
  335. 334.
    Horn, D. B., Standardization of mechanised serum alkaline phosphatase determinations, Clin. Chim. Acta, 37, 43, 1972.Google Scholar
  336. 335.
    Wilkinson, J. H., Boutwell, J. H., and Winsten, S., Evaluation of a new system for the kinetic measurement of serum alkaline phosphatase, Clin. Chem., 15, 487, 1969.Google Scholar
  337. 336.
    Thiers, R. E., and Oglesby, K. M., The precision, accuracy and inherent errors of automatic continuous flow methods, Clin. Chem., 10, 246, 1964.Google Scholar
  338. 337.
    Anonymous, Enzyme analyzers-Enzyme tests, Lab World, 24, 1977.Google Scholar
  339. 338.
    Burnett, R. W., Accurate estimation of standard deviations for quantitative methods used in clinical chemistry, Clin. Chem., 21, 1935, 1975.Google Scholar
  340. 339.
    Skinner, A. G., and Wilding, P., An evaluation of the Greiner Selective Analyzer and its role in the clinical laboratory, Ann. Clin. Biochem., 12, 182, 1975.Google Scholar
  341. 340.
    Westgard, J. O., Carey, R. N., Feldbruegge, D. H., and Jenkins, L. M., Performance studies on the technicon “SMAC” analyzer Precision and comparison of values with methods in routine laboratory service, Clin. Chem., 22, 489, 1976.Google Scholar
  342. 341.
    Ellis, G., Quality control of serum alkaline phosphatase assays Project report and discussion of some factors affecting the assay, Ann. Clin. Biochem., 13, 327, 1976.Google Scholar
  343. 342.
    Hardin, E., Passey, R. B., Gillum, R. L., Fuller, J. B., and Lawrence, D., Clinical laboratory evaluation of the Perkin-Elmer KA-150 enzyme analyzer, Clin. Chem., 22, 434, 1976.Google Scholar
  344. 343.
    Teasdale, P. R., A report on the regional quality control of serum alkaline phosphatase, Ann. Clin. Biochem., 10, 57, 1973.Google Scholar
  345. 344.
    Whitehead, T. P., Browning, D. M., and Gregory, A., A comparative survey of the results of analyses of blood serum in clinical chemistry laboratories in the United Kingdom, J. Clin. Pathol., 2(5, 435, 1973.Google Scholar
  346. 345.
    Jansen, A. P., Van Kampen, E. J., Leijnse, B., Meijers, C. A. M., and Van Munster, P. J. J., Experience in the Netherlands with an external quality control and scoring system for clinical chemistry laboratories, Clin. Chim. Acta, 74, 191, 1977.Google Scholar
  347. 346.
    Stròmme, J. H., and Eldjarn, L., Surveys, of the routine work of clinical chemical laboratories in 116 Scandinavian hospitals, Scand. J. Clin. Lab. Invest., 25, 213, 1970.Google Scholar
  348. 347.
    Stròmme, J. H., and Eldjarn, L., Results and interpretation of the 4th and 5th inter-Scandinavian survey of clinical chemical laboratory analyses (1970–1971), Scand. J. Clin. Lab. Invest. Suppl., 118, 27, 1971.Google Scholar
  349. 348.
    Stromme, J. H., Bjornstad, P., and Eldjarn, L., Improvement in the quality of enzyme determinations by Scandinavian Laboratories upon introduction of Scandinavian recommended methods, Scand. J. Clin. Lab. Invest., 36, 505, 1976.Google Scholar
  350. 349.
    National Bureau of Standards, NBS Standard Reference Materials, NBS SP-260 Supplement, National Bureau of Standards, Washington, D.C., 1977.Google Scholar
  351. 350.
    Wilkinson, J. H., and Vodden, A. V., Phenolphthalein monophosphate as a substrate for serum alkaline phosphatase An appraisal, Clin. Chem., 12, 701, 1966.Google Scholar
  352. 351.
    Christen, P., Vallee, B. L., and Simpson, R. T., Sequential chemical modifications of tyrosyl residues in alkaline phosphatase of Escherichia coli, Biochemistry, 10, 1377, 1971.Google Scholar
  353. 352.
    Signer, E. R., Non-heritable factors in gene expression, Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, 1963.Google Scholar
  354. 353.
    Radin, N., What is a standard?, Clin. Chem., 13, 55, 1967.Google Scholar
  355. 354.
    Harkness, D. R., Studies on human placental alkaline phosphatase. I. Purification and crystallization, Arch. Biochem. Biophys., 126, 503, 1968.Google Scholar
  356. 355.
    Ghosh, N. K., and Fishman, W. H., Purification and properties of molecular-weight variants of human placental alkaline phosphatase, Biochem. J., i05, 779, 1968.Google Scholar
  357. 356.
    American Association for Clinical Chemistry, Standards vs. serum control materials, Clin. Chem., 13, 1107, 1967.Google Scholar
  358. 357.
    Hafkenscheid, J. C. M., and Jansen, A. P., Standardization of the alkaline phosphatase determination with human placental phosphatase, Clin. Chim. Acta, 59, 63, 1975.Google Scholar
  359. 358.
    Babson, A. L., Can enzyme standards be manufactured?, Paper presented at American Association of Clinical Chemists, Symposium on Standardization of Laboratory Procedures, Albany, New York, June 7, 1968.Google Scholar
  360. 359.
    Bretaudiere, J.-P., and Bailly, M., Use and limitations of “controls” in enzyme activity measurements, in Proceedings of the Second International Symposium on Clinical Enzymology (Tietz, N. W., Weinstock, A., and Rodgerson, D. O., eds.), p. 227, American Association for Clinical Chemistry, Washington, D.C., 1976.Google Scholar
  361. 360.
    Latner, A. L. and Hodson, A. W., Human liver alkaline phosphatase purified by affinity chromatography, ultracentrifugation and polyacrylamide-gel electrophoresis, Biochem. J., 159, 697, 1976.Google Scholar
  362. 361.
    Daigle, G., and Petitclerc, C., Human liver alkaline phosphatase a reference material for serum enzyme quality control, Clin. Chem., 23,1161,1977 (Abstr. No. 225).Google Scholar
  363. 362.
    Bowers, G. N., Jr., and Kelley, M. L., Unpublished, 1977.Google Scholar
  364. 363.
    Bowers, G. N., Jr., Standardization efforts in clinical enzymology, Enzyme Symposium, 28th National Meeting, AACC, Clin. Chem., 22, 1143, 1976 (abstract).Google Scholar
  365. 364.
    Bergmeyer, H. U., Standardization of enzyme assay, Clin. Chem., 18, 1305, 1972.Google Scholar
  366. 365.
    Zittle, C. A., Manometric determination of phosphomonoesterase (alkaline phosphatase), J. Franklin Inst., 245, 265, 1948.Google Scholar
  367. 366.
    Schneider, S., and Ullman, E. F., A kinetic assay for alkaline phosphatase activity by use of electron spin resonance spectroscopy, Clin. Chem., 11, 655, 1971 (abstract).Google Scholar
  368. 367.
    Mushak, P., Taylor, J. S., and Coleman, J., Proton hyperflne splitting in the ESR spectra of a stable hydroxynitroxide and its esters, Biochim. Biophys. Acta, 261, 332, 1972.Google Scholar
  369. 368.
    Akaboshi, M., Kawai, K., and Waki, A., Application of activation analysis for determining alkaline phosphatase activity in Tetrahymena, Anal. Biochem., 46, 683, 1972.Google Scholar
  370. 369.
    Ohlmeyer, P., and Shatas, R., Heat of hydrolysis of some phosphate compounds, Arch. Biochem. Biophys., 56, 411, 1952.Google Scholar
  371. 370.
    Monk, P., and Wadso, I., Flow microcalorimetry as an analytical tool in biochemistry and related areas, Acta Chem. Scand., 23, 29, 1969.Google Scholar
  372. 371.
    Miller, I. R., Britten, J. S., and Blank, M., Polarographic assay of p-nitrophenylphosphatase activity, Anal. Biochem., 50, 84, 1972.Google Scholar
  373. 372.
    Keyes, M. H., Electrochemical potentiometric method for selectively determining alkaline phosphatase content in aqueous fluids, United States Patent 3,896,008, July 22, 1975.Google Scholar
  374. 373.
    Schill, W. B., and Schumacher, G. F. B., Radial diffusion in gel for microdetermination of enzymes. I. Muramidase, alpha-amylase, DNAase I, RNAase A, acid phosphatase and alkaline phosphatase, Anal. Biochem., 46, 502, 1972.Google Scholar
  375. 374.
    King, E. J., and Campbell, D. M., International enzyme units An attempt at international agreement, Clin. Chim. Acta, 6, 301, 1961.Google Scholar
  376. 375.
    Lundsteen, E., and Vermehren, E., A micro-method for the estimation of phosphatases in blood plasma, Enzymologia, 1, 273, 1936.Google Scholar
  377. 376.
    Sigma Chemical Company, The colorimetric determination of phosphatase, acid, alkaline and prostatic in serum or other fluids at 400–420 mu, Sigma Chemical Co., St. Louis, Missouri, 1971 (Sigma Technical Bulletin No. 104).Google Scholar
  378. 377.
    The International System of Units (SI), A translation of Le Système International d’Unités (SI) (Page, C. H., and Vigoureux, P., eds.), National Bureau of Standards Special Publication 330, Washington, D.C., 1976.Google Scholar
  379. 378.
    International Union of Pure and Applied Chemistry and International Union of Biochemistry, Enzyme Nomenclature, Elsevier, Amsterdam, 1973.Google Scholar
  380. 379.
    Iino, S., Abe, K., Oda, T., Suzuki, H., and Sugiura, M., A new method of radioimmunoassay for human placental alkaline phosphatase, Clin. Chim. Acta, 42, 161, 1972.Google Scholar
  381. 380.
    Jacoby, B., and Bagshawe, K. D., A radioimmunoassay for placental-type alkaline phosphatase, Cancer Res., 32, 2413, 1972.Google Scholar
  382. 381.
    Forman, D. T., Moss, D. W., and Whitaker, K. B., Determination of human placental alkaline phosphatase by an electroimmunoassay (“Rocket”) technique, Clin. Chim. Acta, 68, 287, 1976.Google Scholar
  383. 382.
    Merrill, D., Hartley, T., and Claman, H. N., Electroimmunodiffusion (EID) A simple, rapid method for quantitation of immunoglobulins in dilute biological fluids, J. Lab. Clin. Med., 69, 151, 1967.Google Scholar
  384. 383.
    Laurell, C.-B., Electroimmuno assay, Scand. J. Clin. Lab. Invest., 29, Suppl. 124, 21, 1972.Google Scholar
  385. 384.
    Coleman, C. M., and Stroje, R., Thymolphthalein monosphosphate as substrate for automated alkaline phosphatase determinations, in Automation in Analytical Chemistry (Skeggs, L. T., éd.), p. 575, Medial, New York, 1966.Google Scholar
  386. 385.
    Van Belle, H., DeBroe, M. E., and Wieme, R. J., L-p-Bromotetramisole, a new reagent for use in measuring placental or intestinal isoenzymes of alkaline phosphatase in human serum, Clin. Chem., 23, 454, 1977.Google Scholar
  387. 386.
    Nagamine, M., and Ohkuma, S., Serum alkaline phosphatase isoenzymes linked to immunoglob-ulin G, Clin. Chim. Acta, 65, 39, 1975.Google Scholar
  388. 387.
    Bodansky, A., Paradoxical increase of phosphatase activity in preserved serum, Proc. Soc. Exp. Biol. Med., 29, 1292, 1932.Google Scholar
  389. 388.
    Culbreth, P. H., Duncan, I. W., and Burtis, C. A., 4-Nitrophenol in 4-nitrophenyl phosphate, a substrate for alkaline phosphatase, as measured by paired-ion high-performance liquid chromatography, Clin. Chem., 23, 2288, 1977.Google Scholar
  390. 389.
    Fujita, H., Über die Mikrobestimmung der Blutphosphatase,Biochem. (Tokyo), 30, 69, 1939.Google Scholar
  391. 390.
    Biggs, A. I., A spectrophotometric determination of the dissociation constants of p-nitrophenol and papaverine, Trans. Faraday Soc., 50, 880, 1954.Google Scholar
  392. 391.
    Goodwin, J. F., Quantification of serum inorganic phosphorus, phosphatase, and urinary phosphate without preliminary treatment, Clin. Chem., 16, 776, 1970.Google Scholar
  393. 392.
    Widdowson, G. M., Performance specifications for instruments used in enzyme activity measurements, in Second International Symposium on Clinical Enzymology (Tietz, N. W., Weinstock, A., and Rodgerson, D. O., eds.), p. 277, American Association for Clinical Chemistry, Washington, D.C., 1976.Google Scholar
  394. 393.
    Public Health Service, List of Test Kits for Clinical Laboratories, p. 15, U.S. Department of Health, Education, and Welfare, Center for Disease Control, Atlanta, Georgia, 1971.Google Scholar
  395. 394.
    Passey, R., Gillum, R. L., Giles, M. L., and Fuller, J. B., Evaluation of the Beckman “System TR Enzyme Analyzer,” Clin. Chem., 21, 1107, 1975.Google Scholar
  396. 395.
    Rand, R. N., Practical spectrophotometric standards, Clin. Chem., 15, 839, 1969.Google Scholar
  397. 396.
    Bogdan, D., and Bishop, C., Differences between manufacturer-assigned values and observed values of alkaline phosphatase activity in a commercial SMA calibration serum, Clin. Chem., 20, 1244, 1974.Google Scholar
  398. 397.
    Steele, B. W., Comparative effects of DE A versus AMP buffer on alkaline phosphatase isoenzymes, Clin. Chem., 22, 1221, 1976.Google Scholar
  399. 398.
    McComb, R. B., Fundamentals of the chemistry of alkaline phosphatase and their relation to the measurement of alkaline phosphatase activity in the laboratory, in 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
  400. 399.
    Cohen, S. R., and Wilson, I. B., Measurement of the zinc dissociation constants of alkaline phosphatase from Escherichia coli by equilibration with zinc ion buffers, Biochemistry, 5, 904, 1966.Google Scholar
  401. 400.
    McComb, R. B., Unpublished, 1974.Google Scholar
  402. 401.
    Bowers, G. N., Jr., and McComb, R. B., Unpublished, 1975.Google Scholar
  403. 402.
    McComb, R. B., Kelley, M. L., and Bowers, G. N., Jr., Unpublished, 1966.Google Scholar
  404. 403.
    McComb, R. B., and Montwell, M., Unpublished, 1976.Google Scholar
  405. 404.
    Blumenfeld, T. A., Hertelendy, W. G., and Ford, S. H., Simultaneously obtained skin-puncture serum, skin-puncture plasma, and venous serum compared and effects of warming the skin before puncture, Clin. Chem., 23, 1705, 1977.Google Scholar
  406. 405.
    McComb, R. B., Unpublished, 1972.Google Scholar
  407. 406.
    O’Kell, R. T., Knepper, D. F., Mantzey, L., and Elliott, J. R., Effect of drugs on results of laboratory tests, Clin. Chem., 18, 1039, 1972.Google Scholar
  408. 407.
    Thiers, R. E., Automation and online computers, in Clinical Chemistry, 2nd ed. (Henry, R. J., Cannon, D. C., and Winkelman, J. W., eds.), p. 209, Harper & Row, Hagerstown, Maryland, 1974.Google Scholar
  409. 408.
    O’Leary, N. D., and Jacob, R., Instability of serum alkaline phosphatase activity in glycine buffer at 31°C, Med. Lab. Sci., 34, 49, 1977.Google Scholar
  410. 409.
    Munan, L., Kelly, A., and Petitclerc, C., Population serum enzyme patterns Age-sex dependencies, Clin. Biochem., 9, 1, 1976.Google Scholar
  411. 410.
    Bowers, G. N., Jr., McComb, R. B., and Kelley, M. L., Standardization of alkaline phosphatase activity measurements The molar absorbtivity of p-nitrophenol in various solution environments, Clin. Chem., 24, 1001, 1978 (abstract).Google Scholar
  412. 411.
    Bannister, A., and Foster, R. L., Enzymatic estimation of protein-ligand association parameters, Anal. Biochem., 82, 185, 1977.Google Scholar
  413. 412.
    Pekelharing, J. M., and Leijnse, B., Initial activity and inactivation of alkaline phosphatase in different lots of buffer, Clin. Chim. Acta, 85, 335, 1978.Google Scholar
  414. 413.
    Williamson, J. A., and Thompson, J. C., An impurity in the buffer 2-amino-2-methyl-l-propanol, which correlates with depression of measured alkaline phosphatase activity, Clin. Chem., 24, 1611, 1978.Google Scholar
  415. 414.
    Rej, R., and Bretaudière, J. P., Personal communication, 1978.Google Scholar
  416. 415.
    Crofton, P. M., and Smith, A. F., The properties and clinical significance of some electrophoretically slow forms of alkaline phosphatase, Clin. Chim. Acta, 83, 235, 1978.Google Scholar
  417. 416.
    Vinet, B., Zizian, L., and Gauthier, B., Characteristics of the inhibition of serum alkaline phos-phatase by theophylline, Clin. Biochem. (Ottawa), 11, 57, 1978.Google Scholar
  418. 417.
    Tanishima, K., Minamikawa, Y., Yokogawa, N., and Takeshita, M., Protective effect of glycerol against the increase in alkaline phosphatase activity of lyophilized quality-control serum, Clin. Chem., 23, 1873, 1977.Google Scholar
  419. 418.
    National Committee for Clinical Laboratory Standards, Proposed standard PSC-5 Methodo-logical principles for establishing principal assigned values to calibrators, Final Report Draft, 7J7J77, p. 7, National Committee for Clinical Laboratory Standards, Villanova, Pennsylvania, 1977.Google Scholar
  420. 419.
    Société Française de Biologie Clinique, Comité de Standardisation, Commission Enzymologie, Ann. Biol. Clin., 35, 271, 1977.Google Scholar
  421. 420.
    Mangum, B. W., and Thornton, D. D., Determination of the triple-point temperature of gallium, Metrologia, 1979 (in press).Google Scholar
  422. 421.
    National Committee for Clinical Laboratory Standards, PSC-7, Guidelines for Kinetic Analysis, Draft 3, Sept. 1978, National Committee for Clinical Laboratory Standards, Villanova, Pennsylvania, 1978.Google Scholar
  423. 422.
    Statistical Vocabulary, ISO 3534, International Organization Standardization, Geneva, Switzerland, 1978.Google Scholar
  424. 423.
    Vocabulary of Legal Metrology, PD6461, pp. 4.2.1 and 8.1. 9, British Standards Institute, London, 1971.Google Scholar
  425. 424.
    Bowers, G. N., Jr., McComb, R. B., Christensen, R. G., and Schaffer, R., High-purity 4-nitro- phenol. Preparation, characterization and specification for its use as a spectrophotometric reference material, Clin. Chem, 1979, submitted for publication.Google Scholar
  426. 425.
    Bowers, G. N., Jr. and McComb, R. B., Unpublished, 1979.Google Scholar

Copyright information

© Plenum Press, New York 1979

Authors and Affiliations

  • Robert B. McComb
    • 1
  • George N. BowersJr.
    • 1
  • Solomon Posen
    • 2
  1. 1.Hartford HospitalHartfordUSA
  2. 2.Sydney HospitalSydneyAustralia

Personalised recommendations