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).
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).
Morgan, William T., The binding and transport of heure by hemopexin, Ann. Clin. Res. 8 (suppl.): 223–232 (1976).
Muller-Eberhard, U., Hemopexin, N. Engl. J. Med. 283: 1090–1094 (1970).
Conway, T. P., and Muller-Eberhard, U., Interaction of hemopexin with water-soluble porphyrine, Arch. Biochem. Biophys. 172: 558–564 (1976).
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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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DOI: https://doi.org/10.1007/978-1-4684-3584-9_10
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