Reiss G H, Ranney H M, Shaklai N
J Clin Invest. 1982 Nov;70(5):946-52. doi: 10.1172/jci110706.
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.
利用膜包埋探针的荧光强度变化研究了血红蛋白C(Hb C)与红细胞膜的相互作用。将pH 6.0和pH 6.8条件下Hb C对膜的亲和力与正常血红蛋白(Hb A)的进行了比较。提供了稳态和动力学数据。pH 6.8时Hb C对红细胞膜的亲和力似乎比Hb A大约高五倍。Hb C和Hb A与膜的结合在大致相同程度上是可逆的。带3膜蛋白的细胞质部分被认为是两种血红蛋白的结合位点。pH值在6.8至7.0时Hb C与膜的结合表明该反应可能在生理条件下发生。