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肌肉收缩的调节:肌钙蛋白及其组分与肌动蛋白和原肌球蛋白的结合。

Regulation of muscle contraction: bindings of troponin and its components to actin and tropomyosin.

作者信息

Hitchcock S E

出版信息

Eur J Biochem. 1975 Mar 17;52(2):255-63. doi: 10.1111/j.1432-1033.1975.tb03993.x.

Abstract

The bindings of troponin components to actin and tropomyosin has been studied by cosedimentation with actin and affinity chromatography. It is shown that troponin binds to actin and tropomyosin in the presence and absence of calcium but the binding to actin is sensitive to ionic strength. Troponin-I + C binds to actin-tropomyosin in the absence of calcium but not to actin or tropomyosin alone. Troponin-I binds to actin and the binding is improved in the presence of tropomyosin even though troponin-I does not bind to tropomyosin alone. Troponin-C does not bind to actin or tropomyosin. The results suggest that the binding of troponin by actin is influenced by tropomyosin. A model of regulation by troponin is proposed.

摘要

通过肌动蛋白共沉降和亲和层析研究了肌钙蛋白各组分与肌动蛋白和原肌球蛋白的结合情况。结果表明,无论有无钙离子存在,肌钙蛋白均可与肌动蛋白和原肌球蛋白结合,但与肌动蛋白的结合对离子强度敏感。在无钙离子存在时,肌钙蛋白-I + C可与肌动蛋白-原肌球蛋白结合,但不能单独与肌动蛋白或原肌球蛋白结合。肌钙蛋白-I可与肌动蛋白结合,且在有原肌球蛋白存在时结合作用增强,尽管肌钙蛋白-I不能单独与原肌球蛋白结合。肌钙蛋白-C不与肌动蛋白或原肌球蛋白结合。这些结果提示,原肌球蛋白会影响肌动蛋白对肌钙蛋白的结合。据此提出了肌钙蛋白调节模型。

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