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. 1982 Nov;70(5):946–952. doi: 10.1172/JCI110706

Association of hemoglobin C with erythrocyte ghosts.

G H Reiss, H M Ranney, N Shaklai
PMCID: PMC370307  PMID: 6752202

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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