Haptoglobins: Hemoglobin Binding

  • Samuel Natelson
  • Ethan A. Natelson


Certain proteins appear in the plasma in increased amounts during inflammatory reactions. These are often referred to as the acute phase reactants.(1) See Section 5.7. Generally, these proteins are glycoproteins synthesized in the parenchymal cells of the liver which contain substantial amounts of carbohydrate attached to the protein molecule. They are precipitable by adding about 150 times the volume of 95% ethanol to serum.(2) The C-reactive protein of serum is a typical example (see Section 5.7.1).


Haptoglobin Level Serum Haptoglobin Hemoglobin Binding Serum Haptoglobin Level Human Haptoglobin 
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Selected Reading

  1. Hwang, P. K., and Greer, J., Identification of residues involved in the binding of hemoglobin alpha chains to haptoglobin, J. Biol. Chem. 254: 2265–2270 (1979).Google Scholar
  2. Hooper, D. C., Reed, R. A., and Peacock, A. C., A haptoglobin radioassay based on binding to solid phase hemoglobin, Anal. Biochem. 93: 355–360 (1979).CrossRefGoogle Scholar
  3. Putnam, F. W., Haptoglobin, in Plasma Proteins, Vol. II, F. W., Putnam, Ed., Academic Press, New York (1975), pp. 1–50.Google Scholar
  4. Giblett, E., Haptoglobin, in Structure and Function of the Plasma Proteins, A. C. Allison, Ed., Plenum Press, New York (1974).Google Scholar
  5. Kirk, R. L., The haptoglobin groups, in Man, Monographs in Human Genetics, Vol. IV, L. Beckman, and S. Hauge, Eds., S. Karger, New York (1968).Google Scholar
  6. Giblett, E. R., Genetic Markers in Human Blood, Blackwell, Oxford (1969).Google Scholar
  7. Pintera, J., The biochemical, genetic and clinicopathological aspects of Haptoglobin, Ser. Haematol. 4 (2): 1–183 (1971).Google Scholar
  8. Sutton, H. E., Haptoglobins, Progr. Med. Genet. 7: 163–216 (1970).Google Scholar
  9. Herman-Boussier, G., Preparation and Physical and Chemical Properties of Human Haptoglobins, Foulon, Paris (1960).Google Scholar
  10. Nyman, M., Serum haptoglobin, Scand. J. Clin. Lab. Invest. 20: 33 (1967).Google Scholar


  1. 1.
    Ward, A. M., Cooper, E. H., and Houghton, A. L., Acute phase reactant proteins in prostatic cancer, Br. J. Urol. 49: 411–418 (1977).CrossRefGoogle Scholar
  2. 2.
    Menini, E., Falholt, W., and Louis, P., Seromucoid and protein-bound hexoses in serum, Acta Med. Scand. 160: 315–322 (1958).CrossRefGoogle Scholar
  3. 3.
    Polonovski, M., and Jayle, M. F., Existence in the blood plasma of a substance which activates the peroxidase activity of hemoglobin, Compt. Rend. Soc. de Biol. 129: 457–460 (1938).Google Scholar
  4. 4.
    Nagel, R. L., and Gibson, Q. H., The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin, J. Biol. Chem. 246: 69–73 (1971).Google Scholar
  5. 5.
    Waks, M., and Alfsen, A., Structural studies of haptoglobins. II. Reversible dissociation into subunits, of Hp 1–1 and Hp2–2, Arch. Biochem. 123: 133–144 (1968).CrossRefGoogle Scholar
  6. 6.
    Connell G. E., Dixon, G. H., and Smithies, O., Genetics-subdivision of the three common haptoglobin types based on “hidden” differences, Nature 193: 505–506 (1962).CrossRefGoogle Scholar
  7. 7.
    Smithies, O., Connell, G. E., and Dixon, G. H., Inheritance of haptoglobin subtypes, Am. J. Hum. Genet. 14: 14–21 (1962).Google Scholar
  8. 8.
    Bong-Sop Shim, and Beam, A. G., Immunological and biochemical studies on serum haptoglobin, J. Exp. Med. 120: 611–628 (1964).CrossRefGoogle Scholar
  9. 9.
    Burrows, S., and Hosten, E. B., Serum haptoglobin automated method applied to patient screening, Am. J. Clin. Pathol. 45: 634–638 (1966).Google Scholar
  10. 10.
    Pastewka, J. V., Reed, R. A., Ness, A. T., and Peacock, A. C., An improved haptoglobin subtyping procedure using polyacrylamide gel electrophoresis: Haptoglobin gene frequency distribution among a group of blood bank donors, Anal. Biochem. 51: 152–162 (1973).CrossRefGoogle Scholar
  11. 11.
    Morawiecka, B., and Mejbaum-Katzenellenbogen, W., The quantitative determination of human seromucoid fractions in paper electrophoresis, Clin. Chim. Acta 7: 722–728 (1962).CrossRefGoogle Scholar
  12. 12.
    Malchy, B., Rorstad, O., and Dixon, G. H., The half-molecule of haptoglobin: Studies on the product obtained by the selective cleavage of a haptoglobin disulfide, Can. J. Biochem, 51: 265–273 (1973).Google Scholar
  13. 13.
    Nagel, R. L., and Ranney, H. M., Haptoglobin binding capacity of certain abnormal hemoglobins, Science 144: 1014–1015 (1964).CrossRefGoogle Scholar
  14. 14.
    Pintera, J., The biochemical, genetic, and clinico-pathological aspects of haptoglobins, Ser. Haematol 4: 1–183 (1971).Google Scholar
  15. 15.
    Fuller, G. M., Rasco, M. A., McCombs, M. L., Barnett, D. R., and Bowman, B. H., Subunit composition of haptoglobin 2–2 polymers, Biochemistry 12: 253–258 (1973).CrossRefGoogle Scholar
  16. 15a.
    Barnett, D. R., Kurosky, A., Fuller, G. M., Kim, H. H., Rasco, M. A., and Bowman, B. H., Structural characterization and genetic variation of haptoglobin, Protides Biol. Fluid Proc. 22: 589–596 (1975).Google Scholar
  17. 16.
    Black, J. A., and Dixon, G. H., Amino acid sequence of the alpha chains of human haptoglobins, Nature 218: 736–741 (1968).CrossRefGoogle Scholar
  18. 17.
    Malchy, B., and Dixon, G. H., Correction to the amino acid sequence of the a chain of human haptoglobin, Can. J. Biochem. 51: 321–322 (1973)CrossRefGoogle Scholar
  19. 18.
    Giblett, E. R., Haptoglobin system, Ser. Haematol. 1: 3–20 (1968).Google Scholar
  20. 19.
    Heimburger, N., Heide, K., Haupt, H., and Schultze, H. E., Structural analysis of human serum proteins, Clin. Chim. Acta. 10: 293–307 (1964).CrossRefGoogle Scholar
  21. 20.
    Ng, A., Owen, J. A., and Padanyi, R., Haptoglobins in pleural and ascitic fluids, Clin. Chim. Acta 8: 145–148 (1963).CrossRefGoogle Scholar
  22. 21.
    Murray, R. K., Connell, G. E., and Pert, J. H., The role of haptoglobin in the clearance and distribution of extracorpuscular hemoglobin, Blood 17: 45–53 (1961).Google Scholar
  23. 22.
    Haupt, H., and Heide, K., Crystallization of haptoglobin 1–1 from human serum, Blut 20: 1–4 (1970).CrossRefGoogle Scholar
  24. 23.
    Javid, J., Human serum haptoglobins: A brief review, Semin. Hematol. 4: 35–52 (1967).Google Scholar
  25. 24.
    Smithies, O., Chromosomal rearrangements and protein structure, Cold Spring Harbor Symp. Quant. Biol. 29: 309–319 (1964).CrossRefGoogle Scholar
  26. 25.
    Giblett, E., Haptoglobin, in Structure and Function of the Plasma Proteins, A. C. Allison, Ed., Plenum, New York (1974).Google Scholar
  27. 26.
    Cleve, H., and Herzog, P., Phenotype variations of haptoglobin Johnson types, Humangenetik 7: 218–224 (1969).CrossRefGoogle Scholar
  28. 27.
    Cleve, H., Gordon, S., Bowman, B. H., and Beam, A. G., Comparison of the tryptic peptides and amino acid composition of the beta polypeptide chains of the three common haptoglobin phenotypes, Am. J. Hum. Genet. 19: 713–721 (1967).Google Scholar
  29. 28.
    Gerbeck, C. M., Bezkorovainy, A., and Rafelson, M. E., Jr., Glycopeptides obtained from human haptoglobin 2–1 and 2–2, Biochemistry 6: 403–411 (1967).CrossRefGoogle Scholar
  30. 29.
    Kurosky, A., Han-Hwa, K., Barnett, D. R., Rasco, M., Touchstone, B., and Bowman, B. H., Comparison of the primary structure of the fi-chain of haptoglobin with serine proteases, Protides Biol. Fluid Proc. 22: 597–601 (1975).Google Scholar
  31. 30.
    Kurosky, A., Barnett, D. R., Rasco, M. A., Lee, T.-H., and Bowman, B. H., Evidence of homology between the fl-chain of human haptoglobin and the chymotrypsin family of serine proteases, Biochem. Genet. 11: 279–293 (1974).CrossRefGoogle Scholar
  32. 30a.
    Kurosky, A., Kim, H-H., and Touchstone, B., Comparative sequence analysis of the N-terminal region of rat, rabbit, and dog haptoglobin fi-chains, Comp. Biochem. Physiol. 55: 453–459 (1976).Google Scholar
  33. 31.
    Kurosky, A., Hay, R. E., Kim, H-H, Touchstone, B., Rasco, M. A., and Bowman, B. H., Characterization of the cyanogen bromide fragments of the ß chain of human haptoglobin, Biochemistry 15: 5326–5336 (1976).CrossRefGoogle Scholar
  34. 31a.
    Malchy, B., and Dixon, G. H., Studies on the interchain disulfides of human haptoglobin, Can. J. Biochem. 51: 219–264 (1973).Google Scholar
  35. 32.
    Cheftel, R. I., Cloarec, L., Moretti, J., and Jayles, M-F., Structure of glycopeptides obtained by proteolysis of human haptoglobin, Bull. Soc. Chim. Biol. 47: 385–393 (1965).Google Scholar
  36. 33.
    Cheftel, R. I., Parnaudeau, M. A., Bourrillon, R., and Moretti, J., Structure of the haptoglobin of the rabbit. Preparation and properties of the glycopeptides, Eur. J. Biochem. 9: 585–590 (1969).CrossRefGoogle Scholar
  37. 34.
    Nagel, R. L., Rothman, M. C., Bradley, T. B., and Ranney, H. M., Comparative haptoglobin binding properties of oxyhemoglobin and deoxyhemoglobin, J. Biol. Chem. 240: 4543–4545 (1965).Google Scholar
  38. 35.
    Nagel, R. L., and Gibson, Q. H., Kinetics and mechanism of complex formation between hemoglobin and haptoglobin, J. Biol. Chem. 242: 3428–3434 (1967).Google Scholar
  39. 36.
    Gordon, S., and Beam, A. G., Hemoglobin binding capacity of isolated haptoglobin polypeptide chains, Proc. Soc. Exp. Biol. 121: 846–850 (1966).Google Scholar
  40. 37.
    Chiancone, E., Alfsen, A., Ioppolo, C., Vecchini, P., Finazzi, A. A., Wyman, J., and Antonini, E., Studies on the reaction of haptoglobin with haemoglobin and haemoglobin chains, J. Mol. Biol. 34: 347–356 (1968).CrossRefGoogle Scholar
  41. 38.
    Lockhart, W. L., and Smith, D. B., Effect of maleylation and amidination of hemoglobin on its haptoglobin and oxygen reactions, Canad. J. Biochem. 49: 148–153 (1971).CrossRefGoogle Scholar
  42. 39.
    Peacock, A. C., Pastewka, J. V., Reed, R. A., and Ness, A. T., Haptoglobinhemoglobin interaction. Stoichiometry, Biochemistry 9: 2275–2279 (1970).Google Scholar
  43. 40.
    Gordon, S., and Beam, A. G., Hemoglobin binding capacity of isolated haptoglobin polypeptide chains, Proc. Soc. Exp. Biol. Med. 121: 846–850 (1966).Google Scholar
  44. 41.
    Alfson, A., Chiancone, E., Wyman, J., and Antonini, E., Studies on the reaction of haptoglobin with hemoglobin and hemoglobin chains. II. Kinetics of complex formation, Biochim. Biophys. Acta 200: 76–80 (1970).Google Scholar
  45. 42.
    Chiao, M. T., and Bezkorovainy, A., Interaction of modified haptoglobin with hemoglobin, Biochim. Biophys. Acta 263: 60–69 (1972).Google Scholar
  46. 43.
    Kawamura, K., Kagiyama, S., Ogawa, A., and Yanese, T., Kinetics of peroxidase activity, absorption spectra and oxygen affinity of human hemoglobin-haptoglobin 1–1 complexes, Biochim. Biophys. Acta 285: 22–27 (1972).Google Scholar
  47. 44.
    Kirk, R. L., The Haptoglobin Groups in Man, Karger, Basel (1968).Google Scholar
  48. 45.
    Renwick, J. H., and Marshall, H., A new type of human haptoglobin Hp 2–1D, Ann. Hum. Genet. 29: 389–390 (1966).CrossRefGoogle Scholar
  49. 46.
    Shim, B. S., Jin, K. S., and Cleve, H., Marburg immunologic reactivity of haptoglobin: Evidence for a beta-chain mutation, Proc. Soc. Exp. Biol. Med. 126: 221–224 (1967).Google Scholar
  50. 47.
    Constans, J., Richard, P., and Vian, M., Relationship between Hp1S and Hp2 gene frequencies among human populations, Hum. Hered. 28: 328–334 (1978).CrossRefGoogle Scholar
  51. 48.
    Robson, E. B., Glen-Bott, A. M., Cleghorn, T. E., and Harris, H., Some rare haptoglobin types, Ann. Human Genet. 28: 77–86 (1964).CrossRefGoogle Scholar
  52. 49.
    Sutton, H. E., and Karp, G. W., Jr., Variations in heterozygous expression at the haptoglobin locus, Am. J. Hum. Genet. 16: 419–434 (1963).Google Scholar
  53. 50.
    Sutton, H. E., The haptoglobins, Progr. Med. Genet. 7: 163–216 (1970).Google Scholar
  54. 51.
    Cleve, H., and Deicher, H., Haptoglobin “Marburg”: Investigation of a rare genetic haptoglobin variant with two different phenotypes within a family, Humangenetik 1: 537–550 (1965).CrossRefGoogle Scholar
  55. 52.
    Javid, J., Haptoglobin 2–1 Bellevue, a haptoglobin ß-chain mutant, Proc. Natl. Acad. Sci. USA 57: 920–924 (1967).CrossRefGoogle Scholar
  56. 53.
    Shim, B-S., and Beam, A. G., The distribution of haptoglobin subtypes in various populations, including subtype patterns in some non-human primates, Am. J. Hum. Genet. 16: 477–383 (1964).Google Scholar
  57. 54.
    Giblett, E. R., Variant haptoglobin phenotypes, Cold Spring Harbor Symp. Quant. Biol. 29: 321–326 (1964).CrossRefGoogle Scholar
  58. 55.
    Schwerd, W., and Sander, I., Gene defects in the haptoglobin system, Blut. 15: 99–100 (1967).CrossRefGoogle Scholar
  59. 56.
    Gitlin, D., and Biasucci, A., Development of gamma G, gamma A, gamma M, beta 1C-, beta 1A, Cl esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, alpha 1-antitrypsin, orosomucoid, beta-lipoprotein, alpha 2-macroglobulin, and prealbumin in the human conceptus, J. Clin. Invest. 48: 1433–1446 (1969).CrossRefGoogle Scholar
  60. 57.
    Garby, L., Noyes, W. D., Studies on hemoglobin metabolism. I. The kinetic properties of the plasma hemoglobin pool in normal man, J. Clin. Invest. 38: 1479–1483 (1959).CrossRefGoogle Scholar
  61. 58.
    Noyes, W. D., and Garby, L., Rate of haptoglobin in synthesis in normal man., Scand. J. Clin. Lab. Invest. 20: 33–38 (1967).Google Scholar
  62. 59.
    Funakoshi, S., Oomura, T., Ohshiro, T., and Hong, S. D., Haptoglobin: Its isolation and clinical significance, Prog. Clin. Biol. Res. 5: 397–414 (1976).Google Scholar
  63. 60.
    Giblett, E. R., Haptoglobin: A review, Vox Sang 6: 513–524 (1961).CrossRefGoogle Scholar
  64. 61.
    Nyman, M., Serum haptoglobin: Methodological and clinical studies, Scand. J. Clin. Lab. Invest. 11: suppl. 1–169 (1959).Google Scholar
  65. 62.
    Neuhaus, O. W., and Sogoian, V. P., Presence of haptoglobin in synovial fluid, Nature 192: 558–559 (1961).CrossRefGoogle Scholar
  66. 63.
    Niedermeier, W., Cross, R., and Beetham, W. P., Jr., The concentration of haptoglobin in synovial fluid of patients with rheumatoid arthritis, Arthritis Rheum, 8: 355–360 (1965).CrossRefGoogle Scholar
  67. 64.
    Marnay, A., Haptoglobinuria in nephrotic syndromes, Nature 191: 74–75 (1961).CrossRefGoogle Scholar
  68. 65.
    Barnett, D. R., Lee, T-H., and Bowman, B. H., Amino-acid sequence of the human haptoglobin ß-chain. I. Amino and carboxyl-terminal sequences, Biochemistry 11: 1189–1194 (1972).CrossRefGoogle Scholar
  69. 66.
    Wada, T., Oara, H., Watanabe, K., Kinoshita, H., and Nishio, H., Auto-radiographic study on the site of uptake of the haptoglobin-hemoglobin complex, J. Retic. Soc. 8: 185–193 (1970).Google Scholar
  70. 67.
    Peters, J. H., and Alper, C. A., Haptoglobin synthesis. II. Cellular localization studies, J. Clin. Invest. 45: 314–320 (1966).CrossRefGoogle Scholar
  71. 68.
    Keene, W. R., and Jandl. J. H., The sites of hemoglobin catabolism, Blood 26: 705–719 (1965).Google Scholar
  72. 69.
    Hershko, C., Cook, J. D., and Finch, C. A., Storage iron kinetics. II. The uptake of hemoglobin iron by hepatic parenchymal cells, J. Lab. Clin. Med. 80: 624–634 (1972).Google Scholar
  73. 70.
    John, D. W., and Miller, L. L., Regulation of net biosynthesis of serum albumin and acute phase plasma proteins, J. Biol. Chem. 244: 6134–6142 (1969).Google Scholar
  74. 71.
    Shim, B-S., Increase in serum haptoglobin stimulated by prostaglandins, Nature 259: 326–327 (1976).CrossRefGoogle Scholar
  75. 72.
    Voelkel, E. F., Levine, L., Alper, C. A., and Tashjian, A. H. Jr., Acute phase reactants ceruloplasmin and haptoglobin and their relationship to plasma prostaglandins in rabbits bearing VX2 carcinoma, J. Exp. Med., 1078–1088 (1978).Google Scholar
  76. 74.
    Owen, J. A., Smith, R., Padanyi, R., and Martin, J., Serum haptoglobin in disease, Clin. Sci. 26: 1–6 (1964).Google Scholar
  77. 75.
    Gerson, J., Evans, A. E., and Rosen, F. S., The prognostic value of acute phase reactants in patients with neuroblastoma, Cancer 40: 1655–1658 (1977).CrossRefGoogle Scholar
  78. 76.
    Laurell, C. B. and Nyman, M., Studies on the serum haptoglobin level in hemoglobinemia and its influence on renal excretion of hemoglobin, Blood 12: 493–506 (1957).Google Scholar
  79. 77.
    Lathem, W., Davis, B. B., Zweig, P. H., and Dew, R., The demonstration and localization of renal tubular reabsorption of hemoglobin by stop flow analysis, J. Clin. Invest. 39: 840–845 (1960).CrossRefGoogle Scholar
  80. 78.
    Lowenstein, J., Faulstick, D. A., Yiengst, M. J., and Shock, N. W., The glomerular clearance and renal transport of hemoglobin in adult males, J. Clin. Invest. 40: 1172–1177 (1961).CrossRefGoogle Scholar
  81. 79.
    Snellman, O., and Sylven, B., Haptoglobin acting as a natural inhibitor of cathepsin B activity, Nature 216: 1033 (1967).CrossRefGoogle Scholar
  82. 80.
    Dobryszycka, W., and Lisowska, E., Effect of degradation on the chemical and biological properties of haptoglobin, I. Products of tryptic digestion, Biochim. Biophys. Acta 121: 42–50 (1966).CrossRefGoogle Scholar
  83. 81.
    Culliford, B. J., and Wraxall, B. G. D., Haptoglobin types in dried bloodstains, Nature 211: 872–873 (1966).CrossRefGoogle Scholar
  84. 82.
    Galatius-Jensen, F., The use of serum haptoglobin patterns in cases of disputed paternity, Meth. Forensic Sci. 1: 497–538 (1962).Google Scholar
  85. 83.
    Hever, O., Haptoglobin subtypes in Hungary, Hum. Hered. 26: 324–326 (1976).CrossRefGoogle Scholar
  86. 84.
    Krauss, S., Chrott, M., and Sarcione, E. J., Haptoglobin metabolism in Hodgkin’s disease, Am. J. Med. Sci. 252: 184–191 (1966).CrossRefGoogle Scholar
  87. 85.
    Valeri, C. R., Bond, J. C., Fowler, K., and Sobucki, J., Quantitation of serum hemoglobin-binding capacity using cellulose acetate membrane electrophoresis, J. Clin. Chem. 11: 581–588 (1965).CrossRefGoogle Scholar
  88. 86.
    Schleyer, F., and Schaible, P., Demonstration of haptoglobin types by means of electrophoresis in polyacrylamide gel, Z. Klin. Chem. 5: 32–34 (1967).Google Scholar
  89. 87.
    Ferris, T. G., Easterling, R. E., Nelson, K. J., and Budd, R. E., Determination of serum-hemoglobin binding capacity and haptoglobin-type by acrylamide gel, Am. J. Clin. Path. 46: 385–389 (1966).Google Scholar
  90. 88.
    Culliford, B. J., Haptoglobin and transferrin in forensic bloodstains, Nature 198: 796–797 (1963).CrossRefGoogle Scholar
  91. 89.
    Hodgson, R., and Sewell, P., Determination of serum haptoglobin concentration: a simple rapid gel filtration method, J. Med. Lab. Technol. 22: 130–134 (1965).Google Scholar
  92. 90.
    Lionettii, F. J., Valeri, C. R., Bond, J. C., and Fortier, N. L., Measurement of hemoglobin binding capacity of human serum or plasma by means of dextran gels, J. Lab. Clin. Med. 64: 519–528 (1964).Google Scholar
  93. 91.
    Moretti, J., Waks, M., and Jayle, R. M., Determination of haptoglobin by Technicon Autoanalyser, Ann. Biol. Clin. (Paris) 25: 149–154 (1967).Google Scholar
  94. 92.
    Kickler, T. S., Fong, P. F., Johnson, G. F., and Solomon, H. M., Kinetic determination of serum haptoglobin with a centrifugal analyzer, Clin. Chem. 22: 1962–1967 (1976).Google Scholar
  95. 93.
    Vincent, J. P., Borel, J. P., Engler, R., and Jayle, M. F., Determination of haptoglobin with the aid of the LKB S600 reaction rate analyzer, Ann. Biol. Clin. 33: 45–49 (1975).Google Scholar
  96. 94.
    Standing, S., and Price, C. P., A kinetic method for the determination of haptoglobin as hemoglobin binding capacity, Clin. Chim. Acta 66: 393–403 (1976).CrossRefGoogle Scholar
  97. 95.
    Connell, G. E., and Smithies, O., Human haptoglobins: Estimation and purification, Biochem. J. 39: 1013–1019 (1961).Google Scholar
  98. 96.
    Braun, H. J., and Aly, F. W., Problems in the quantitative estimation of human serum haptoglobin by single radial immunodiffusion, Clin. Chim. Acta 26: 588–590 (1969).CrossRefGoogle Scholar
  99. 97.
    Kluthe, R., Faul, J., and Heimpl, H., Quantitative estimation of human serum haptoglobins by an immunological method, Nature 205: 93–94 (1965).CrossRefGoogle Scholar
  100. 98.
    Roy, R. B., Shaw, R. W., and Connell, G. E., A simple method for the quantitative determination of serum haptoglobin, J. Lab. Clin. Med. 74: 698–704 (1969).Google Scholar
  101. 99.
    Galatius-Jensen, F., Rare phenotypes in the Hp system, Acta Genet. 8: 248–255 (1958).Google Scholar
  102. 100.
    Shim, B. S., Lee, T-H., and Kang, Y-S., Immunological and biochemical investigations of human serum haptoglobin, composition of haptoglobinhemoglobin intermediates, hemoglobin binding sites and presence of additional alleles for the ß chain, Nature 207: 1264–1267 (1965).CrossRefGoogle Scholar
  103. 101.
    Giblett, E. R., Uchida, I., and Brooks, L. E., Two rare haptoglobin phenotypes 1-B and 2-B, containing a previously undescribed a polypeptide chain, Am. J. Hum. Genet. 18: 448–453 (1966).Google Scholar
  104. 102.
    Giblett, E. R., Haptoglobin types in American Negroes, Nature 183: 192–193 (1959).CrossRefGoogle Scholar
  105. 103.
    Giblett, E. R., and Steinberg, A. G., The inheritance of the serum haptoglobin types in American Negroes: Evidence for a third allele Hp2M, Am. J. Hum. Genet. 12: 160–169 (1960).Google Scholar
  106. 104.
    Murray, R. F., Robinson, J. C., Dublin, T. D., Pitt, E. L., and Visnich, S., Observations on the inheritance of hypohaptoglobinemia, Acta Genet. 16: 113–121 (1966).Google Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Samuel Natelson
    • 1
  • Ethan A. Natelson
    • 2
  1. 1.Department of Environmental Practice, College of Veterinary MedicineUniversity of TennesseeKnoxvilleUSA
  2. 2.University of Texas Medical School and St. Joseph HospitalHoustonUSA

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