An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments.
An in vitro study of the interactions of skeletal muscle M-protein and creatine kinase with myosin and its subfragments.
复制标题
骨骼肌 M 蛋白和肌酸激酶与肌球蛋白及其亚片段相互作用的体外研究。
DOI：
10.1016/s0022-2836(83)80077-1
复制
发表时间：
1983
影响因子：
5.6
通讯作者：
Lowey,S
中科院分区：
文献类型：
--
作者：
Woodhead,JL;Lowey,S
据报道，位于骨骼肌m波段的两个蛋白是m蛋白（mr16万）和肌酸激酶（mr83万）。我们从成年鸡胸肌中分离纯化了这些蛋白，并研究了它们与肌凝蛋白、重肌凝蛋白、轻肌凝蛋白和亚片段-2的体外相互作用，以便更全面地了解这些蛋白在骨骼肌m带中的作用。实验采用分析性超离心、亲和层析和电镜技术，在接近生理pH值和离子强度的条件下进行，在这种条件下，已知m带蛋白与肌原纤维原位紧密结合。我们的研究结果表明，这种相互作用是弱或缺席体外。讨论了我们的结果与其他几项研究结果之间的差异。我们的结论是，为了观察体外相互作用，可能需要额外的成分，这些成分类似于完整肌原纤维中存在的相互作用。
Two proteins reported to be located in the M-band of skeletal muscle are M-protein (Mr160,000) and creatine kinase (Mr83,000). We have isolated and purified these proteins from adult chicken pectoralis muscle, and have studied theirin vitrointeractions with myosin, heavy meromyosin, light meromyosin and subfragment-2 in order to obtain a fuller understanding of the role these proteins play in the M-band of skeletal muscle. Experiments using the techniques of analytical ultracentrifugation, affinity chromatography and electron microscopy were carried out near physiological pH and ionic strength, under which conditions the M-band proteins are known to be firmly bound to the myofibrilin situ. The results of our studies indicate that such interactions are either weak or absentin vitro. Discrepancies between our results and those from several other studies are discussed. We conclude that additional components may be required in order to observe interactionsin vitrowhich are similar to those present in the intact myofibril.