人血小板47000道尔顿蛋白对肌动蛋白聚合的调节作用。
Modulation of actin polymerization by 47,000-dalton protein of human platelets.
作者信息
Hashimoto K, Hashimoto K, Im T, Tatsumi N, Okuda K, Yukioka M
机构信息
Second Department of Biochemistry, Osaka City University Medical School, Japan.
出版信息
Biochem Int. 1987 Apr;14(4):759-67.
We purified 47,000-dalton proteins from both thrombin-stimulated and unstimulated human platelets. The purity of the protein was almost 80% on SDS-polyacrylamide gel electrophoresis. The protein obtained from unstimulated platelets strongly inhibited actin gelation when its molar ratio to actin was 1:200 or higher. The protein obtained from thrombin-stimulated platelets had no inhibitory activity. The results suggest that the 47,000-dalton protein modulates actin polymerization through phosphorylation.
我们从凝血酶刺激和未刺激的人血小板中纯化了47000道尔顿的蛋白质。该蛋白质在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上的纯度几乎为80%。当从未刺激的血小板中获得的蛋白质与肌动蛋白的摩尔比为1:200或更高时，它强烈抑制肌动蛋白凝胶化。从凝血酶刺激的血小板中获得的蛋白质没有抑制活性。结果表明，47000道尔顿的蛋白质通过磷酸化调节肌动蛋白聚合。
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