Tsutou A, Nakamura S, Negami A, Mizuta K, Hashimoto E, Yamamura H
Biochem Biophys Res Commun. 1985 Jan 16;126(1):544-50. doi: 10.1016/0006-291x(85)90640-0.
Porcine uterine smooth muscle phosphorylase kinase has been partially purified. The enzyme was activated about 1.5-2.0-fold by exogenous calmodulin. Half maximal stimulation was observed at about 100 nM calmodulin. The activation was dependent on calcium and was maximum at pH 7.5 in the range of pH from 6 to 9. This activation was completely abolished by 100 microM trifluoperazine. The result suggested that unlike slow and cardiac muscles, phosphorylase kinase of uterine smooth muscle showed similar response to calmodulin with that of fast muscle. The physiological role of the calcium and calmodulin-dependent activation of myometrium phosphorylase kinase is briefly discussed.
猪子宫平滑肌磷酸化酶激酶已被部分纯化。该酶被外源性钙调蛋白激活约1.5 - 2.0倍。在约100 nM钙调蛋白时观察到半最大刺激。这种激活依赖于钙,在pH 6至9范围内,pH 7.5时激活作用最大。100 microM三氟拉嗪可完全消除这种激活。结果表明,与慢肌和心肌不同,子宫平滑肌的磷酸化酶激酶对钙调蛋白的反应与快肌相似。本文简要讨论了子宫肌层磷酸化酶激酶钙和钙调蛋白依赖性激活的生理作用。