Phosphorylation of the 20,000-dalton light chain of myosin of intact arterial smooth muscle in rest and in contraction.
Phosphorylation of the 20,000-dalton light chain of myosin of intact arterial smooth muscle in rest and in contraction.
复制标题
完整动脉平滑肌在休息和收缩时的 20,000 道尔顿肌球蛋白轻链的磷酸化。
DOI：
10.1016/s0021-9258(18)50543-3
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发表时间：
1979
期刊：
影响因子：
--
通讯作者：
K. Bárány
中科院分区：
文献类型：
--
作者：
J. T. Barron;M. Bárány;K. Bárány
当动脉肌肉在含有[32 P]正磷酸盐的37 ℃生理盐溶液中孵育时，发现完整猪颈动脉的20，000-道尔顿肌球蛋白轻链被快速标记。在完整的肌肉轻链磷酸化有一个显着的要求Ca 2+，并依赖于被动张力施加到肌肉。去甲肾上腺素或氯化钾诱导的挛缩与轻链磷酸化的伴随增加有关。
The 20,000-dalton myosin light chain of intact pig carotid arteries was found to be rapidly labeled when the arterial muscle was incubated in physiological salt solution at 37 degrees C containing [32P]orthophosphate. Light chain phosphorylation in the intact muscle had a marked requirement for Ca2+ and was dependent upon the passive tension applied to the muscle. Norepinephrine- or KCl-induced contractures were associated with concomitant increases in light chain phosphorylation.