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

H Benedikter, G Knopki, P Renz
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引用次数: 0

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.

牛血小板磷脂酰肌醇特异性磷脂酶C。钙调素抑制剂的抑制作用——ATP和ADP的激活作用。
牛血小板粗提物的磷脂酶c活性在mM范围内受到钙调素抑制剂氟非那嗪和卡咪唑的强烈抑制,并被ATP和ADP激活,而不被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'-三磷酸和α, β -亚甲基腺苷5'-二磷酸也表现出激活作用,从而表明它是一种变构效应。ATP对磷脂酶c活性的刺激在一些部分纯化的粗血小板提取物中也可以检测到,但在进一步纯化酶时就会消失。
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