来自牛血小板的磷脂酰肌醇特异性磷脂酶C。受钙调蛋白抑制剂抑制——被ATP和ADP激活。

Phosphatidylinositol-specific phospholipase C from bovine blood platelets. Inhibition by calmodulin-inhibitors--activation by ATP and ADP.

作者信息

Benedikter H, Knopki G, Renz P

出版信息

Z Naturforsch C Biosci. 1985 Jan-Feb;40(1-2):68-72. doi: 10.1515/znc-1985-1-214.

DOI:10.1515/znc-1985-1-214

Abstract

The phospholipase C-activity in crude extracts of bovine blood platelets is strongly inhibited by the calmodulin-inhibitors fluphenazine and calmidazolium in the mM range, and activated by ATP and ADP, but not by AMP. The activating effect is also shown by the nonhydrolysable ATP- and ADP-analogs alpha,beta- and beta,gamma-methyleneadenosine 5'-triphosphate and alpha,beta-methyleneadenosine 5'-diphosphate, thus indicating that it is an allosteric effect. The stimulation of the phospholipase C-activity by ATP is also detectable in some partially purified fractions of the crude platelet extract, but it is abolished on further purification of the enzyme.

摘要

牛血小板粗提物中的磷脂酶C活性在毫摩尔范围内受到钙调蛋白抑制剂氟奋乃静和氯咪巴唑的强烈抑制，并被ATP和ADP激活，但不被AMP激活。不可水解的ATP和ADP类似物α,β-和β,γ-亚甲基腺苷5'-三磷酸以及α,β-亚甲基腺苷5'-二磷酸也显示出激活作用，因此表明这是一种别构效应。在粗血小板提取物的一些部分纯化组分中也可检测到ATP对磷脂酶C活性的刺激作用，但在酶进一步纯化后这种刺激作用消失。