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在ADP和凝血酶刺激的血小板细胞骨架中存在原肌球蛋白的证据。

Evidence for the presence of tropomyosin in the cytoskeletons of ADP- and thrombin-stimulated blood platelets.

作者信息

Pho D B, Vasseur C, Desbruyeres E, Olomucki A

出版信息

FEBS Lett. 1984 Jul 23;173(1):164-8. doi: 10.1016/0014-5793(84)81039-x.

Abstract

Stimulation of porcine platelets with ADP or thrombin and subsequent analyses of their cytoskeletons by SDS-polyacrylamide gel electrophoresis have shown the presence of a 30.5-kDa polypeptide in the cytoskeletons of activated as well as aggregated platelets. This polypeptide comigrates with pure porcine platelet tropomyosin in SDS gels, their mobilities being similarly and markedly decreased in the presence of 6 M urea. One-dimensional peptide mapping after limited proteolysis by Staphylococcus aureus protease gives the same pattern for pure tropomyosin and the 30.5-kDa polypeptide. This latter may thus be identified as the porcine platelet tropomyosin subunit, the role of which may not be solely structural.

摘要

用二磷酸腺苷(ADP)或凝血酶刺激猪血小板,随后通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)分析其细胞骨架,结果显示在活化及聚集血小板的细胞骨架中存在一种30.5 kDa的多肽。该多肽在SDS凝胶中与纯猪血小板原肌球蛋白迁移率相同,在6 M尿素存在下,它们的迁移率同样显著降低。经金黄色葡萄球菌蛋白酶有限水解后的一维肽图显示,纯原肌球蛋白和30.5 kDa多肽具有相同的图谱。因此,后者可被鉴定为猪血小板原肌球蛋白亚基,其作用可能不仅限于结构方面。

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