Cholesterol modulation of (Na+ + K+)-ATPase ATP hydrolyzing activity in the human erythrocyte.
Cholesterol modulation of (Na+ + K+)-ATPase ATP hydrolyzing activity in the human erythrocyte.
复制标题
胆固醇对人红细胞中 (Na K )-ATP 酶 ATP 水解活性的调节。
DOI：
10.1016/0005-2736(83)90366-8
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Yeagle,PL
中科院分区：
文献类型：
--
作者：
Yeagle,PL
用超声鸡蛋卵磷脂/胆固醇囊泡和鸡蛋卵磷脂/胆碱囊泡孵育完整细胞，对人红细胞膜胆固醇含量进行了修饰。（Na++ K+）-ATP酶ATP水解活性随细胞膜胆固醇含量的变化而变化。高膜胆固醇抑制atp酶的活性，低膜胆固醇激活该酶的活性。最有可能的抑制机制被认为包括直接的胆固醇-蛋白质相互作用，导致低活性构象。瓦巴因结合研究表明，这种抑制不是由于膜上酶的损失。
The cholesterol content of human erythrocyte membranes has been modified by incubation of intact cells with sonicated egg phosphatidylcholine/cholesterol vesicles and with egg phosphatidylcholine vesicles. (Na++ K+)-ATPase ATP hydrolyzing activity was measured as a function of membrane cholesterol content. High membrane cholesterol inhibits the ATPase activity of the enzyme and low membrane cholesterol activates that enzyme activity. The most likely mechanism of inhibition is suggested to comprise direct cholesterol-protein interactions which lead to a low activity conformation. Ouabain binding studies show that the inhibition is not due to a loss of enzyme from the membrane.