Citations to this article
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.
Authors
G H Reiss, H M Ranney, N Shaklai
Total citations by year
Citations to this article in year 2008 (2)
| Title and authors | Publication | Year |
|---|---|---|
|
Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease
E Nagababu, ME Fabry, RL Nagel, JM Rifkind |
Blood Cells, Molecules, and Diseases | 2008 |
|
Phase separation and crystallization of hemoglobin C in transgenic mouse and human erythrocytes
JE Canterino, O Galkin, PG Vekilov, RE Hirsch |
Biophysical Journal | 2008 |
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