Phosphorylation of the 18,000-dalton light chain of myosin during a single tetanus of frog muscle.
Phosphorylation of the 18,000-dalton light chain of myosin during a single tetanus of frog muscle.
复制标题
青蛙肌肉单次破伤风期间肌球蛋白 18,000 道尔顿轻链的磷酸化。
DOI：
10.1016/s0021-9258(17)40117-7
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发表时间：
1977
期刊：
影响因子：
--
通讯作者：
M. Bárány
中科院分区：
文献类型：
--
作者：
K. Bárány;M. Bárány
利用注射了[32P]正磷酸盐的肝蛙解剖肌肉，研究了肌肉收缩引起的蛋白质中32P含量的变化。唯一发现的重大变化是18000道尔顿轻链肌球蛋白的放射性；在单次破伤风中，与静止肌肉相比，增加了85%至90%。每mol轻链增加约0.4 mol 32P。在咖啡因引起的完整肌肉挛缩中也发现了这种轻链放射性的增加。据推测，电刺激或咖啡因治疗引起的肌浆中Ca2+浓度的增加激活了肌球蛋白轻链激酶，使18000道尔顿轻链磷酸化。
Changes in the 32P content of proteins due to muscle contraction were investigated, using muscles dissected from liver frogs injected with [32P]orthophosphate. The only significant change found was in the radioactivity of the 18,000-dalton light chain of myosin; during a single tetanus, an increase of 85 to 90% occurred as compared to the resting muscle. This increase corresponded to about 0.4 mol of 32P per mol of light chain. The same increase in radioactivity of this light chain was also found upon caffeine-induced contracture of the intact muscle. It is postulated that the increased Ca2+ concentration in the sarcoplasm resulting from electrical stimulus or caffeine treatment activates the myosin light chain kinase which phosphorylates the 18,000-dalton light chain.