Yeagle P L
Biochim Biophys Acta. 1983 Jan 5;727(1):39-44. doi: 10.1016/0005-2736(83)90366-8.
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.
通过将完整细胞与超声处理的卵磷脂酰胆碱/胆固醇囊泡以及卵磷脂酰胆碱囊泡一起孵育，对人红细胞膜的胆固醇含量进行了修饰。测定了（Na + + K +）-ATP酶的ATP水解活性与膜胆固醇含量的关系。高膜胆固醇抑制该酶的ATP酶活性，低膜胆固醇则激活该酶活性。最可能的抑制机制被认为包括导致低活性构象的直接胆固醇-蛋白质相互作用。哇巴因结合研究表明，这种抑制不是由于酶从膜上丢失所致。
