Selective Binding of Met-Hemoglobin to Erythrocytic Membrane: A Possible Involvement in Red Blood Cell Aging
It is well known that in vivo and under normal physiological conditions intraerythrocytic hemoglobin may exist in three different forms represented by oxygenated, deoxygenated and partially oxidized hemoglobin (1–4). Apart from the first two derivatives whose relative proportions are continuously changing during the oxygenation deoxygenation cycle, met-hemoglobin is normally present at a steady-state level of about 1%.
KeywordsG6PD Deficiency Human Hemoglobin Hemoglobin Solution Hemoglobin Molecule Progressive Oxidation
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- 1.E. Antonini and M. Brunori, “Hemoglobin and myoglobin in their reactions with ligands”, A. Neuberger and E. L. Tatum, North-Holland Publ. Co., Amsterdam (1971).Google Scholar
- 9.C. E. Moya, S. Shah and T. M. Sodeman, The erythrocyte, in: “Sodeman’s Pathologic Physiology”, 7th edition W. B. Saunders, Baltimore (1985).Google Scholar
- 15.R. Scatena, S. G. Condò, M. E. Clementi, M. Corda, M. T. Sanna, M. G. Pellegrini and B. Giardina, Methemoglobin and enzymatic reduction systems: physiological and pathological implications, Ital. J. Biochem. (1990) in press.Google Scholar
- 16.M. Sharabani, B. Plotkin and I. Aviram, Lipid peroxidation in red blood cell membranes, Cell. Molec. Biol 30:329 (1984).Google Scholar
- 20.C. Rice-Evan and E. Baysal, Iron-mediated oxidative stress in erythrocytes, Biochem. J. 244:191 (1987).Google Scholar