外源性或内源性磷脂酰肌醇特异性磷脂酶C对血小板膜结合乙酰胆碱酯酶和芳基酰胺酶的溶解作用。

The solubilization of platelet membrane-bound acetylcholinesterase and aryl acylamidase by exogenous or endogenous phosphatidylinositol specific phospholipase C.

作者信息

Majumdar R, Balasubramanian A S

出版信息

Biochem Pharmacol. 1985 Dec 1;34(23):4109-15. doi: 10.1016/0006-2952(85)90202-3.

Abstract

Phosphatidylinositol specific phospholipase C from Staphylococcus aureus could solubilize acetylcholinesterase up to 55% from sheep platelets in the presence of ethylenediaminetetra acetic acid (EDTA). The endogenous phosphatidylinositol specific phospholipase C of platelets activated by deoxycholate (at 3-5 mM) could also solubilize the enzyme to a similar extent. The solubilized enzyme could be further purified to apparent homogeneity by affinity chromatography without the use of any detergents. It is suggested that phosphatidylinositol specific phospholipase C will be a useful tool in the solubilization of acetylcholinesterase from mammalian sources and its purification free of detergents. The present study also demonstrates the parallel behaviour of acetylcholinesterase and aryl acylamidase in platelets confirming their identity.

摘要

在乙二胺四乙酸（EDTA）存在的情况下，金黄色葡萄球菌的磷脂酰肌醇特异性磷脂酶C能从绵羊血小板中溶解高达55%的乙酰胆碱酯酶。经脱氧胆酸盐（3 - 5 mM）激活的血小板内源性磷脂酰肌醇特异性磷脂酶C也能将该酶溶解到相似程度。溶解后的酶无需使用任何去污剂，通过亲和层析可进一步纯化至表观均一性。研究表明，磷脂酰肌醇特异性磷脂酶C将是从哺乳动物来源溶解乙酰胆碱酯酶并在无去污剂条件下进行纯化的有用工具。本研究还证实了血小板中乙酰胆碱酯酶和芳基酰胺酶的平行行为，从而确定了它们的同一性。