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Principles of Applied Clinical Chemistry pp 409–427Cite as

Hemopexin: Iron Recycling

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Abstract

There is a significant amount of methemoglobin circulating in human plasma at all times. In this compound, the iron in the iron-porphyrin complex is in the trivalent state and does not participate in oxygen exchange. The prosthetic group is called ferriprotoporphyrin IX. The free base is called hematin, and the chloride salt hemin (see Volume 2, p. 469). Some use the expressions ferriheme for ferriprotoporphyrin IX and ferrihemoglobin to signify methemoglobin.

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  • Zinkham, W. T., Vangrov, J. S., Dixon, S. M., and Hutchinson, J. L., Observations on the rate and mechanism of hemolysis in individuals with Hb-Zurich (Hb-Zurich, HisE7, 63, beta, leads to arg.) concentration of haptoglobin and hemopexin in the serum, Johns Hopkins Med. J. 144: 37–40 (1979).

    Google Scholar 

  • Muller-Eberhard, U., and Lieur, H. H., Hemopexin, the heure binding serum glycoprotein, in Structure and Function of Plasma Proteins, A. C. Allison, Ed., Plenum Press, New York (1974).

    Google Scholar 

  • Morgan, William T., The binding and transport of heure by hemopexin, Ann. Clin. Res. 8 (suppl.): 223–232 (1976).

    Google Scholar 

  • Muller-Eberhard, U., Hemopexin, N. Engl. J. Med. 283: 1090–1094 (1970).

    Article  Google Scholar 

  • Conway, T. P., and Muller-Eberhard, U., Interaction of hemopexin with water-soluble porphyrine, Arch. Biochem. Biophys. 172: 558–564 (1976).

    Article  Google Scholar 

References

  1. Grabar, P., DeVaux St. Cyr., C., and Cleve, H., Presence of ß1,ß-globulin in the perchloric acid extracts of normal human sera, Bull. Soc. Chim. Biol. 42: 853–836 (1960).

    Google Scholar 

  2. Heide, K., Haupt, H., Storiko, K., and Schultze, H. E., On the heure binding capacity of hemopexin, Clin. Chim. Acta 10: 460–469 (1964).

    Article  Google Scholar 

  3. Hanstein, A., and Muller-Eberhard, U., Concentration of serum hemopexin in healthy children and adults and in those with a variety of hematological disorders, J. Lab. Clin. Med. 71: 232–239 (1968).

    Google Scholar 

  4. Neale, F. C., Aber, G. M., and Northam, B. E., The demonstration of intra-vascular haemolysis by means of serum paper electrophoresis and a modification of Schumm’s reaction, J. Clin. Path. 11: 206–219 (1958).

    Article  Google Scholar 

  5. Seery, V. L., Hathaway, G., and Muller-Eberhard, U., Hemopexin of human and rabbit: Molecular weight and extinction coefficient, Arch. Biochem. Biophys. 150: 269–272 (1972).

    Article  Google Scholar 

  6. Morgan, W. T., Capra, J. D., Kehoe, J. M., and Muller-Eberhard, U., Human and rabbit hemopexins: Tryptic peptides and N-terminal sequences, FEBS Lett. 48: 109–113 (1974).

    Article  Google Scholar 

  7. Muller-Eberhard, U., Hemopexin, N. Engl. J. Med. 283: 1090–1094 (1970).

    Article  Google Scholar 

  8. Hrkal, Z., and Muller-Eberhard, U., Partial characterization of the hemebinding serum glycoproteins rabbit and human hemopexin, Biochemistry 10: 1746–1750 (1971).

    Article  Google Scholar 

  9. Rosen, H., and Sears, D. A., Spectral properties of hemopexin-heme: the Schumm test, J. Lab. Clin. Med. 74: 941–945 (1969).

    Google Scholar 

  10. Morgan, W. T., The binding and transport of heme by hemopexin, Ann. Clin. Res. 8 (suppl. 17): 223–232 (1976).

    Google Scholar 

  11. Aber, G. M., and Rowe, D. S., The binding of haematin by serum proteins, Br. J. Haemat. 6: 160–165 (1960).

    Article  Google Scholar 

  12. Allison, A. C., and Rees, W., The binding of haemoglobin by plasma proteins (haptoglobins), Br. Med. J. 2: 1137–1143 (1957).

    Article  Google Scholar 

  13. Bearden, A. J., Morgan, W. T., and Muller-Eberhard, U., Herne complexes of rabbit hemopexin, human hemopexin and human serum albumin: Electron spin resonance and Mossbauer spectroscopic studies, Biophys. Res. Commun. 61: 265–272 (1974).

    Article  Google Scholar 

  14. Morgan, W. T., and Vickery, L. E., Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin, J. Biol. Chem. 253: 2940–2943 (1978).

    Google Scholar 

  15. Hrkal, Z., Vodrâzka, Z., and Kalousek, I., Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin, Eur. J. Biochem. 43: 73–78 (1974).

    Article  Google Scholar 

  16. Morgan, W. T., Muller-Eberhard, U., and Lamola, A. A., Interaction of rabbit hemopexin with bilirubin, Biochim. Biophys. Acta 532: 57–64 (1978).

    Google Scholar 

  17. Kelly, T. R., Klein, R. L., Porquez, J. M., and Homer, G. M., Methemalbumin in acute pancreatitis: An experimental and clinical appraisal, Ann. Surg. 175: 15–18 (1972).

    Article  Google Scholar 

  18. Kodiixek, M., Hrkal, Z., and Vodrâika, Z., On the molecular conformation of human haemopexin. II. Analysis of circular dichroic spectra, Biochim. Biophys. Acta 495: 268–278 (1977).

    Google Scholar 

  19. Kodíitek, M., Hrkal, Z., Suttnar, J., and Vodriiika, Z., On the molecular conformation of human haemopexin. I. Reactivity of the tyrosine and tryptophan side chains, Biochim. Biophys. Acta 495: 260–267 (1977).

    Google Scholar 

  20. Planche, Y., Dautrexvaux, M., and Biserte, G., Change of human hemopexin isoelectric point upon heure binding, FEBS Lett. 78: 291–294 (1977).

    Article  Google Scholar 

  21. Seery, V. L., and Muller-Eberhard, U., Binding of porphyrins to rabbit hemopexin and albumin, J. Biol. Chem. 248: 3796–3800 (1973).

    Google Scholar 

  22. Havez, R., Moschetto, Y., Hayem-Levy, A., and Biserte, G., Alkylation of histidine radicals at the combining site of seromucoid ß1 with hematin, Comfit. Rend. Acad. Sci. (Paris) 265: 585–589 (1967).

    Google Scholar 

  23. Aisen, P., Leibman, A., Harris, D. C., and Moss, T., Human hemopexin: Preparation and magnetic properties, J. Biol. Chem. 249: 6824–6827 (1974).

    Google Scholar 

  24. Seery, V. L., Morgan, W. T., and Muller-Eberhard, U., Interaction of rabbit hemopexin with rose bengal and photooxidation of the rose bengal-hemopexin complex, J. Biol. Chem. 250: 6439–6444 (1975).

    Google Scholar 

  25. Muller-Eberhard, U., and Morgan, W. T., Porphyrin-binding proteins in serum, N.Y. Acad. Sci. 244: 624–650 (1975).

    Article  Google Scholar 

  26. Sears, D. A., Disposal of plasma heure in normal man and patients with intravascular hemolysis, J. Clin. Invest. 49: 5–14 (1970).

    Article  Google Scholar 

  27. Liem, H. H., Hepatic uptake of heure and hemopexin but not albumin, Biochim. Biophys. Acta 343: 546–550 (1974).

    Article  Google Scholar 

  28. Lane, R. S., Rangeley, D. M., Liem, H. H., Wormsley, S., and Muller-Eberhard, U., Plasma clearance of ‘251-labeled haemopexin in normal and haemloaded rabbits, Br. J. Haematol. 25: 533–540 (1973).

    Article  Google Scholar 

  29. Liem, H. H., Spector, J. I., Conway, T. P., Morgan, W. T., and Muller-Eberhard, U., Effect of hemoglobin and hematin on plasma clearance of hemopexin, photo-inactivated hemopexin and albumin, Proc. Soc. Exp. Biol. Med. 148: 519–522 (1975).

    Google Scholar 

  30. Morgan, W. T., Liem, H. H., Sutor, R. P., and Muller-Eberhard, U., Transfer of heure from heme-albumin to hemopexin, Biochim. Biophys. Acta 444: 435–445 (1976).

    Article  Google Scholar 

  31. Biserte, G., Havez, R., and Laturze, J., Electrophoretic characterization and immunology of ß1 seromucoid in human blood serum, Compt. Rend. Soc. Biol. 11: 2061–2066 (1960).

    Google Scholar 

  32. Maines, M. D., Anders, M. W., and Muller-Eberhard, U., Studies on heure transfer from microsomal hemoproteins to heme-binding plasma proteins, Molecular Pharmacology 10: 204–213 (1974).

    Google Scholar 

  33. Gielen, J. E., Goujon, F. M., and Nebert, D. W., Genetic regulation of aryl hydrocarbon: Hydroxylase induction. II-Simple Mendelian expression in mouse tissues in vivo, J. Biol. Chem. 247: 1125–1137 (1972).

    Google Scholar 

  34. Conway, T. P., and Muller-Eberhard, U., Interaction of hemopexin with water-soluble porphyrins, Arch. Biochem. Biophys. 172: 558–564 (1976).

    Article  Google Scholar 

  35. Atzeni, E., Binaghi, F., and Pitzus, F., Haemopexin behaviour in an acute hyperhaemolytic crisis secondary to favism (erythrocyte glucose-6-phosphate dehydrogenase deficiency), Ric. Clin. Lab. 7: 39–43 (1977).

    Google Scholar 

  36. Bunn, H. F., Erythrocyte destruction and hemoglobin catabolism, Semin. Hematol. 9: 3–17 (1972).

    Google Scholar 

  37. Muller-Eberhard, U., and Liem, H. H., Hemopexin, the heme-binding serum ß-glycoprotein, in Structure and Function of Plasma Proteins, Vol. 1, A. C. Allison, Ed., Plenum Press, N.Y. (1974), pp. 35–53.

    Chapter  Google Scholar 

  38. Meiers, H. G., and Ippen, H., Ahemopexinemia in cutanea tarda porphyria, Klin. Wechenschr. 46: 560–561 (1968).

    Article  Google Scholar 

  39. Hershko, C., Annotation: The fate of circulating haemoglobin, Br. J. Haemat. 29: 199–204 (1975).

    Article  Google Scholar 

  40. Warnick, G. R., and Burnham, B. F., Regulation of porphyrin biosynthesis: Purification and characterization of aminolevulinic acid synthase, J. Biol. Chem. 246: 6880–6885 (1971).

    Google Scholar 

  41. Nyman, M., On plasma proteins with heme or hemoglobin binding capacity, Scand. J. Clin. Lab. Invest. 12: 121–130 (1960).

    Article  Google Scholar 

  42. Schultze, H. E., Heide, K., and Haupt, H., Characterization of highly purified hemopexin, Naturwissenschaften 48: 696–697 (1961).

    Article  Google Scholar 

  43. Gitlin, D., and Biasucci, A., Development of yG, yA, yM, ßIC and ßIA esterase inhibitor, ceruloplasmin, transferrin, hemopexin, haptoglobin, fibrinogen, plasminogen, a-I-antitrypsin, orosomucoid, lipoprotein, 2-macroglobulin and prealbumin in the human conceptus, J. Clin. Invest. 48: 1433–1446 (1969).

    Article  Google Scholar 

  44. Weippl, G., Pantlitschko, M., and Hammelmann, C., Hemopexin in cord blood, Clin. Chim. Acta 29: 338 (1970).

    Article  Google Scholar 

  45. Muller-Eberhard, U., and Bashore, R., Assessment of Rh disease by ratios of bilirubin to albumin and hemopexin to albumin in amniotic fluid, N. Engl. J. Med. 282: 1163–1167 (1970).

    Article  Google Scholar 

  46. Swahn, B., Bronnestam, R., and Dencker, S. J., On the origin of the lipoproteins in the cerebrospinal fluid, Neurology 11: 437–440 (1961).

    Article  Google Scholar 

  47. Muller-Eberhard, U., and Cox, K. H., Development of non-specific antibodies to rat hemopexin and albumin Evidence for immunological cross-reactivity with mouse proteins, Comp. Biochem. Physiol. 51: 47–50 (1975).

    Google Scholar 

  48. Thorbecke, G. J., Liem, H. H., Knight, S., Cox, K., and Muller-Eberhard, U., Sites of formation of the serum proteins transferrin and hemopexin, J. Clin. Invest. 52: 725–731 (1973).

    Article  Google Scholar 

  49. Muller-Eberhard, U., and English, E. C., Purification and partial characterization of human hemopexin, J. Lab. Clin. Med. 70: 619–626 (1967).

    Google Scholar 

  50. Shibert, E., Liem, H. H., and Muller-Eberhard, U., Studies on the induction of serum hemopexin by pentobarbitol and polycyclic hydrocarbons, Biochem. Pharmacol. 21: 1753–1761 (1972).

    Article  Google Scholar 

  51. Myrhed, M., Wetterberg, L., and Muller-Eberhard, U., Genetic control of serum hemopexin, Ann. Clin. Res. 8 (suppl. 17): 259–261 (1976).

    Google Scholar 

  52. Sears, D. A., Plasma heme-binding in patients with hemolytic disorders, J. Lab. Clin. Med. 71: 484–494 (1968).

    Google Scholar 

  53. Seager, J., Haemopexin, caeruloplasmin and C3: Effect of diphenylhydantoin, Clin. Chim. Acta 79: 603–606 (1977).

    Article  Google Scholar 

  54. Braun, H. J., and Aly, F. W., Clinical significance of the quantitative serum hemopexin determination in comparison to haptoglobin, Klin. Wochenschr. 49: 451–457 (1971).

    Article  Google Scholar 

  55. Braun, H. J., The significance of immunological hemopexin estimation for the diagnosis of hemolytic pancreatitis, Verhand. Deutsch. Ges. Inn. Med. 78: 1426–1429 (1972).

    Google Scholar 

  56. Bokisch, V. A., Top, F. H., Jr., Russell, P. K., Dixon, F. J., and Muller-Eberhard, H. J., The potential pathogenic role of complement in dengue hemorrhagic shock syndrome, N. Engl. J. Med. 289: 996–1000 (1973).

    Article  Google Scholar 

  57. Murray-Lyon, I. M., Studies on plasma proteins in liver disease using quantitative immunoelectrophoresis, Ph.D. dissertation. University Edinburgh, Scotland (1973).

    Google Scholar 

  58. Muller-Eberhard, U., Liem, H. H., Mathews-Roth, M. M., and Epstein, J. H., Plasma levels of hemopexin and albumin in disorders of porphyrin metabolism, Proc. Soc. Exp. Biol. Med. 146: 694–697 (1974).

    Google Scholar 

  59. Cleve, H., Alexander, K., Mitzkat, H. J., Nissen, P., and Salzmann, I., Serum proteins in diabetes mellitus: Quantitative immunological estimation of acid al-glycoprotein, Gc, a2 macroglobin and hemopexin in diabetics without angiopathy, Diabetologia 4: 48–55 (1968).

    Article  Google Scholar 

  60. Aakanas, W., and Mazurczak, J., The serum immunoelectrophoretic test in patients with Duchenne’s progressive muscular dystrophy: Preliminary report, Life Sci. 5: 247–251 (1966).

    Article  Google Scholar 

  61. Manuel, Y., DeFontaine, M. C., Bourgoin, J. J., Dargent, M., and Sonneck, J. M., Serum hemopexin levels in patients with malignant melanoma, Clin. Chim. Acta 3: 485–486 (1971).

    Article  Google Scholar 

  62. Snyder, S., and Ashwell, G., Quantitation of specific serum glycoproteins in malignancy, Clin. Chim. Acta 34: 449–455 (1971).

    Article  Google Scholar 

  63. Danieli, G. A., and Angelini, C., Duchenne carrier detection, Lancet 2: 90 (1976).

    Article  Google Scholar 

  64. Rowland, L. P., Layzer, R. B., and Kagen, L. J., Lack of some muscle proteins in serum of patients with Duchenne dystrophy, Arch. Neurol. 18: 272–276 (1968).

    Article  Google Scholar 

  65. Miller, S. E., Roses, A. P., and Appel, S. H., Scanning electron microscopy studies in muscular dystrophy, Arch. Neurol. 33: 172–174 (1976).

    Article  Google Scholar 

  66. Muller-Eberhard, U., Liem, H. H., Hanstein, A., and Saarinen, P. A., Studies on the disposal of intravascular heme in the rabbit, J. Lab. Clin. Med. 73: 210–218 (1969).

    Google Scholar 

  67. Ross, J. D., Muller-Eberhard, U., and Carroll, L. A., Pharmacologic induction of serum hemopexin by 3-methylcholanthrene and allylisopropylacetamide, J. Lab. Clin. Med. 75: 694–702 (1970);

    Google Scholar 

  68. Ross, J. D., Muller-Eberhard, U., and Carroll, L. A., Biochem. Biophys. Res. Commun. 41: 186–193 (1970).

    Article  Google Scholar 

  69. Cripps, D. J., Liem, H. H., and Muller-Eberhard, U., Griseofulvin causing hyperhemopexinemia and hepatic proliferation in mice: An in vivo and in vitro study, J. Invest. Dermatol. 68: 82–87 (1977).

    Article  Google Scholar 

  70. Piomielli, S., Davidow, B., Guinee, V. F., Young, P., and Gay, G., The FEP (free erythrocyte porphyrins) test. A screening micromethod for lead poisoning, Pediatrics 51: 254–259 (1972).

    Google Scholar 

  71. Hrkal, Z., Vodrazka, Z., and Rejnkova, J., Purification of human serum hemopexin by chromatography on DEAE-cellulose, J. Chromatogr. 72: 198–201 (1972).

    Article  Google Scholar 

  72. Vretblad, P., and Hjorth, R., The use of wheat-germ lectinsepharose for the purification of human haemopexin, Biochem. J. 167: 759–764 (1977).

    Google Scholar 

  73. Hayem-Levy, A., and Havez, R., Isolation and study of human hemopexin, Clin. Chim. Acta 47: 113–122 (1973).

    Article  Google Scholar 

  74. Suttnar, J., Hrkal, Z., and Vodrazka, Z., Affinity chromatography of serum haemopexin, J. Chromatogr. 131: 453–457 (1977).

    Article  Google Scholar 

  75. Mancini, G., Carbonara, A. O., and Heremans, J. F., Immunochemical quantitation of antigens by single radial immunodiffusion, Int. J. Immunochemistry 2: 235–254 (1965).

    Article  Google Scholar 

  76. Laurell, C. B., Electroimmunoassay, Scand. J. Clin. Lab. Invest. 29 (suppl. 124): 21–23 (1972).

    Article  Google Scholar 

  77. Ganrot, P. 0., Crossed immunoelectrophoresis, Scand. J. Clin. Lab. Invest. 29 (suppl. 124): 39–44 (1972).

    Article  Google Scholar 

  78. Rosen, H., and Sears, D. A., Spectral properties of hemopexin heure: The Schumm test, J. Lab. Clin. Med. 74: 941–945 (1969).

    Google Scholar 

  79. Ursing, B., Clinical and immunoelectrophoretic studies on cerebrospinal fluid in virus meningoencephalitis and bacterial meningitis, Acta Med. Scand. 177 (suppl. 429): 1–99 (1965).

    Google Scholar 

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Authors and Affiliations

  1. Department of Environmental Practice, College of Veterinary Medicine, University of Tennessee, Knoxville, Tennessee, USA

    Samuel Natelson Ph.D.

  2. University of Texas Medical School and St. Joseph Hospital, Houston, Texas, USA

    Ethan A. Natelson M.D.

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  1. Samuel Natelson Ph.D.
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© 1980 Plenum Press, New York

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Natelson, S., Natelson, E.A. (1980). Hemopexin: Iron Recycling. In: Principles of Applied Clinical Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3584-9_10

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