Association of hemoglobin C with erythrocyte ghosts.
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.
D001665:Binding Sites; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006441:Hemoglobin A / Q000378:metabolism; D006444:Hemoglobin C / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D010108:Oxyhemoglobins / Q000378:metabolism / Q000494:pharmacology
D010108:Oxyhemoglobins; D006444:Hemoglobin C; D006441:Hemoglobin A