Binding of 2,3-diphosphoglycerate by spectrin and its effect on oxygen affinity of hemoglobin.
Binding of 2,3-diphosphoglycerate by spectrin and its effect on oxygen affinity of hemoglobin.
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血影蛋白与 2,3-二磷酸甘油酯的结合及其对血红蛋白氧亲和力的影响。
DOI：
10.1152/ajpcell.1978.234.1.c36
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发表时间：
1978
期刊：
影响因子：
--
通讯作者：
H. Ranney
中科院分区：
文献类型：
--
作者：
N. Shaklai;L. Benitez;H. Ranney
血影蛋白是红细胞膜面向胞浆的结构蛋白，本文研究了血影蛋白与血红蛋白的关系。剥离血红蛋白的氧结合特性没有改变的血影蛋白的存在下，但血红蛋白与有机磷酸盐的相互作用减少了血影蛋白的加入。甘油醛3-磷酸脱氢酶（G3 PD），红细胞膜的另一个组成部分，作为对照的存在下，没有改变氧亲和力的剥离血红蛋白或血红蛋白溶液中含有磷酸盐。在pH 7.3下使用凝胶过滤法的结合研究表明2，3-二磷酸甘油酸与血影蛋白的可逆结合。经计算，220，000道尔顿的单位具有7个结合位点，结合常数为1.2 × 10（4）M-1。提出了一种机制，其中血影蛋白可以促进血红蛋白分子到达膜的氧运输。
The relationships between spectrin, a structural protein of the red blood cell (RBC) membrane facing the cytoplasm, and hemoglobin were studied. The oxygen-binding properties of stripped hemoglobin were not altered by the presence of spectrin, but the interaction of hemoglobin with organic phosphates was reduced by the addition of spectrin. The presence of the enzyme glyceraldehyde 3-phosphate dehydrogenase (G3PD), another component of the RBC membrane used as a control, did not change the oxygen affinity of either stripped hemoglobin or of hemoglobin solutions containing phosphates. Binding studies using the gel filtration method at pH 7.3 indicated reversible binding of 2,3-diphosphoglycerate to spectrin. A unit of 220,000 daltons was calculated to have seven binding sites and a binding constant of 1.2 X 10(4) M-1. A mechanism is proposed in which spectrin may facilitate oxygen transport for hemoglobin molecules reaching the membrane.