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Association of Hemoglobin C with Erythrocyte Ghosts

Overview
Journal J Clin Invest
Specialty General Medicine
Date 1982 Nov 1
PMID 6752202
Citations 8
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Abstract

The interaction of hemoglobin C (Hb C) with erythrocyte membranes was studied using changes in fluorescence intensity in a membrane-embedded probe. The affinity of Hb C for the membranes at pH 6.0 and pH 6.8 was compared to that of normal hemoglobin (Hb A). Steady-state and kinetic data were delivered. The affinity of Hb C for the erythrocyte membrane at pH 6.8 appeared to be about five times greater than that of Hb A. The associations of Hb C and Hb A with the membrane were reversible to about the same extent. The cytoplasmic portions of band 3 membrane proteins were suggested to be the binding sites for both hemoglobins. The membrane binding of Hb C at pH values of 6.8 to 7.0 indicates that this reaction may occur under physiological circumstances.

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References
1.
Shaklai N, Yguerabide J, Ranney H . Classification and localization of hemoglobin binding sites on the red blood cell membrane. Biochemistry. 1977; 16(25):5593-7. DOI: 10.1021/bi00644a032. View

2.
Shaklai N, Ranney H . Interaction of hemoglobin with membrane lipids: a source of pathological phenomena. Isr J Med Sci. 1978; 14(11):1152-6. View

3.
Natta C, Muir M . Preferential binding of beta C relative to beta S globin to stroma in hemoglobin SC disease. Hemoglobin. 1980; 4(2):157-63. DOI: 10.3109/03630268009042382. View

4.
Kliman H, Steck T . Association of glyceraldehyde-3-phosphate dehydrogenase with the human red cell membrane. A kinetic analysis. J Biol Chem. 1980; 255(13):6314-21. View

5.
Shaklai N, Abrahami H . The interaction of deoxyhemoglobin with the red cell membrane. Biochem Biophys Res Commun. 1980; 95(3):1105-12. DOI: 10.1016/0006-291x(80)91586-7. View