Synthesis by fast muscle of myosin light chains characteristic of slow muscle in response to long-term stimulation.
Synthesis by fast muscle of myosin light chains characteristic of slow muscle in response to long-term stimulation.
复制标题
快肌合成慢肌特征的肌球蛋白轻链，以响应长期刺激。
DOI：
10.1038/newbio241017a0
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
F. Romanul
中科院分区：
文献类型：
--
作者：
F. Streter;J. Gergely;S. Salmons;S. Salmons;F. Romanul
从兔的慢（红色）骨骼肌中分离的肌球蛋白在几个方面不同于从快（白色）骨骼肌中分离的肌球蛋白。特别地，慢肌肌球蛋白的ATP酶比快肌肌球蛋白的ATP酶显示出更低的比活性，并且与后者不同，慢肌肌球蛋白在碱性pH下不稳定。白色肌肌球蛋白含有三种小亚基，即所谓的轻链，在20，000道尔顿范围内，而来自红色肌肉的肌球蛋白含有两类轻链，其分子量不同于白色肌肉肌球蛋白中的任何轻链1，2。Salmons和Vrbova 3发现，通过连续刺激运动神经数周，可以改变快速肌肉的收缩速度，这会显著减缓收缩和舒张的时间进程。由于Barany4已经表明肌肉的肌球蛋白ATP酶活性与其收缩速度密切相关，因此似乎应该检查从收缩速度已被实验改变的肌肉中提取的肌球蛋白的ATP酶活性和轻链补体中可能明显的变化（如果有的话）。
MYOSIN isolated from slow (red) skeletal muscles of the rabbit differs in several respects from myosin isolated from fast (white) skeletal muscle. In particular the ATPase of slow muscle myosin shows lower specific activity than that of fast muscle myosin and, unlike the latter, is labile at alkaline pH. White muscle myosin contains three kinds of small subunits, the so called light chains, in the 20,000 dalton range, while myosin from red muscle contains two classes of light chains which differ in molecular weight from any of the light chains in white muscle myosin1,2. Salmons and Vrbova3 have found that the contractile speed of a fast muscle can be changed by continuous stimulation of the motor nerve over a period of weeks, which produces a marked slowing of the time course of contraction and relaxation. As Barany4 has shown that the myosin ATPase activity of a muscle correlates closely with its contractile speed, it seemed appropriate to examine what changes, if any, might be evident in the ATPase activity and light chain complement of myosin extracted from muscles whose contractile speed had been altered experimentally.