Protein phosphorylation during spontaneous contraction of smooth muscle.
Protein phosphorylation during spontaneous contraction of smooth muscle.
复制标题
平滑肌自发收缩期间的蛋白质磷酸化。
DOI：
10.1016/0006-291x(80)91209-7
复制
发表时间：
1980
影响因子：
3.1
通讯作者：
R. Gualtieri
中科院分区：
文献类型：
--
作者：
R. Janis;B. Moats;R. Gualtieri
本文研究了大鼠子宫平滑肌自发收缩与蛋白磷酸化的关系。从雌激素为主的大鼠子宫肌条孵育在[32 P]正磷酸盐，然后冷冻在不同水平的等长张力。用凝胶电泳法分离蛋白质，并测定~（32）P掺入量。收缩与一种主要蛋白质（20，000 Mr）的磷酸化有关。这种磷酸化先于最大张力的发展，去磷酸化先于完全的自发松弛。双向凝胶电泳表明，20，000-Mr蛋白是肌球蛋白轻链，它与平滑肌收缩的调节有关。
The relationship between spontaneous contraction and protein phosphorylation of rat uterine smooth muscle was studied. Myometrial strips from estrogen-dominated rats were incubated in [32P]orthophosphate and then frozen at various levels of isometric tension. Proteins were separated by gel electrophoresis and the incorporation of32P was measured. Contraction was associated with the phosphorylation of one major protein (20,000 Mr). This phosphorylation preceded maximal tension development and dephosphorylation preceded complete spontaneous relaxation. Two-dimensional gel electrophoresis indicates that the 20,000-Mrprotein is the myosin light chain which has been implicated in the regulation of smooth muscle contraction.