肾微绒毛膜的外切酶。去污剂的差异增溶作用可预测糖基磷脂酰肌醇膜锚定物。
Ectoenzymes of the kidney microvillar membrane. Differential solubilization by detergents can predict a glycosyl-phosphatidylinositol membrane anchor.
作者信息
Hooper N M, Turner A J
机构信息
Department of Biochemistry, University of Leeds, U.K.
出版信息
Biochem J. 1988 Mar 15;250(3):865-9. doi: 10.1042/bj2500865.
Abstract
The pattern of solubilization of nine kidney microvillar ectoenzymes by a range of detergents distinguished two classes of membrane proteins: those released from the membrane by bacterial phosphatidylinositol-specific phospholipase C and those not so released. The latter group of transmembrane proteins were solubilized efficiently (greater than 80%) by all the detergents examined. In contrast, proteins released by phosphatidylinositol-specific phospholipase C were solubilized effectively only by octyl glucoside, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulphonate and sodium deoxycholate. Octyl glucoside solubilized the amphipathic forms of the ectoenzymes examined, suggesting that this may be a useful detergent in the purification of glycosyl-phosphatidylinositol-anchored ectoenzymes.
摘要
一系列去污剂对九种肾微绒毛外切酶的增溶模式区分出两类膜蛋白
一类是通过细菌磷脂酰肌醇特异性磷脂酶C从膜上释放出来的，另一类则不是。后一组跨膜蛋白能被所有检测的去污剂有效增溶（大于80%）。相比之下，由磷脂酰肌醇特异性磷脂酶C释放的蛋白仅能被辛基葡糖苷、3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸盐和脱氧胆酸钠有效增溶。辛基葡糖苷增溶了所检测外切酶的两亲形式，这表明它可能是纯化糖基磷脂酰肌醇锚定外切酶的一种有用去污剂。
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