Interaction of intestinal disaccharidases with phospholipids: effect of cholesterol.
Interaction of intestinal disaccharidases with phospholipids: effect of cholesterol.
复制标题
肠道二糖酶与磷脂的相互作用：胆固醇的影响。
DOI：
10.1097/00005176-198512000-00019
复制
发表时间：
1985
影响因子：
2.9
通讯作者：
Seetharam,B
中科院分区：
文献类型：
--
作者：
Tiruppathi,C;Alpers,DH;Seetharam,B
虽然大鼠小肠刷状缘dispylidases是最容易溶解的蛋白质组分，脂质-蛋白质相互作用的性质在膜上是不完全理解。使用来自刷状缘膜的卵磷脂级分和合成卵磷脂制备磷脂囊泡。此外，胆固醇刷状缘卵磷脂增强了结合的dispylidases，但不是碱性磷酸酶。胆固醇的合成卵磷脂囊泡的加入增强了结合dispylidases只有当添加以上所使用的卵磷脂的转变温度。最大的影响发生在等摩尔比的卵磷脂胆固醇。磷脂囊泡的结合是独立的电荷或极性头基团的性质，并插入酶，使催化结构域被排除在脂质基质。这些结果表明，膜附着的dispronidases是疏水性的，主要涉及脂肪酰基链和与胆固醇的相互作用。膜相互作用似乎不影响酶的活性。
Although the rat intestinal brush border disaccharidases are the most easily solubilized protein components, the nature of the lipid-protein interactions in the membrane is incompletely understood. Phospholipid vesicles were prepared using the lecithin fraction from brush border membranes and synthetic lecithins. Addition of cholesterol to brush border lecithins enhanced the binding of disaccharidases, but not of alkaline phosphatase. The addition of cholesterol to synthetic lecithin vesicles enhanced the binding of disaccharidases only when added above the transition temperature of the lecithin used. The maximal effect occurred at an equimolar ratio of lecithin to cholesterol. Binding of disaccharidases to phospholipid vesicles was independent of charge or the nature of the polar head group, and the enzyme was inserted so that the catalytic domain was excluded from the lipid matrix. These results demonstrate that membrane attachment of disaccharidases is hydrophobic, involving primarily fatty acyl chains and an interaction with cholesterol. The membrane interaction does not seem to affect enzyme activity.