Postmortem changes in the actin-myosin interaction of rabbit skeletal muscle.
Postmortem changes in the actin-myosin interaction of rabbit skeletal muscle.
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DOI：
10.1093/oxfordjournals.jbchem.a133197
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发表时间：
1981
影响因子：
2.7
通讯作者：
K. Takahashi;F. Nakamura;A. Inoue
中科院分区：
文献类型：
--
作者：
K. Takahashi;F. Nakamura;A. Inoue
死后肌动蛋白-肌球蛋白相互作用的变化进行了研究，通过测定ATP解离的粗丝和细丝的量。在肌肉僵直状态下制备的肌原纤维中，分离的肌丝数量非常少，而在肌肉僵直后储存期间，分离的肌丝数量显著增加。电子显微镜下，从储存的肌肉制备的分离的厚和薄的细丝与新鲜制备的相似，并且没有任何迹象表明任何类型的细丝的蛋白水解降解可以观察到。一种蛋白质，这是释放肌原纤维（可能从Z光盘）上钙+处理似乎是最密切相关的僵硬后的粗丝从细丝的解离。
Postmortem changes in the actin-myosin interaction were studied by determining the amount of thick and thin filaments dissociated by ATP. The amount of separated filaments was very small in myofibrils prepared from muscles in rigor, while it increased markedly during post-rigor storage of muscles. Electron microscopically, separated thick and thin filaments prepared from stored muscles were similar to freshly prepared ones and no signs of proteolytic degradation of either type of filament could be observed. A protein which was released from myofibrils (probably from Z discs) on Ca2+-treatment seemed to be most closely related to the post-rigor dissociation of thick filaments from thin filaments.