Free fatty acids and (Na+,K+)-ATPase: effects on cation regulation, enzyme conformation, and interactions with ethanol.
Free fatty acids and (Na+,K+)-ATPase: effects on cation regulation, enzyme conformation, and interactions with ethanol.
复制标题
游离脂肪酸和 (Na ,K )-ATP 酶:对阳离子调节、酶构象以及与乙醇相互作用的影响。
DOI:
10.1016/0003-9861(84)90456-9
复制
发表时间:
1984
影响因子:
3.9
通讯作者:
Swann,AC
中科院分区:
文献类型:
--
作者:
Swann,AC
Abstract Effects of free fatty acids on parameters of (Na+, K+)-ATPase regulation related to enzyme conformation were examined. Sensitivity to inhibition by free fatty acid increased as the number of double bonds increased. Free fatty acids reduced affinity for K+ or Na+ at their regulatory sites without altering apparent K+ affinity at its high-affinity site, and increased apparent affinity for ATP. The apparent E2 E1 ratio and apparent ΔH and ΔS for the E1–E2 transition were reduced by fatty acid. High K+ or low temperature reduced the sensitivity of enzyme to inhibition by free fatty acid. In the presence of low K+, arachidonic acid potentiated inhibition of phosphatase activity by ethanol. Arachidonic acid alone had little effect on the rate of ouabain binding, but accelerated ouabain binding in the presence of K+. These data suggest that fatty acids alter (Na+, K+)-ATPase by preventing the univalent cation-mediated transition to E2, the K+-sensitive form of enzyme.(Na+, K+)-ATPase could potentially be influenced in vivo by free fatty acids released by phospholipases or during hypoxia, or by changes in membrane lipid saturation.