Association of hemoglobin C with erythrocyte ghosts

G. H. Reiss, H. M. Ranney, N. Shaklai

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

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 derived. 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.

Original languageEnglish
Pages (from-to)946-952
Number of pages7
JournalJournal of Clinical Investigation
Volume70
Issue number5
DOIs
StatePublished - 1982
Externally publishedYes

Fingerprint

Dive into the research topics of 'Association of hemoglobin C with erythrocyte ghosts'. Together they form a unique fingerprint.

Cite this