Zemskova M A, Shur S A, Skolysheva L K, Vul'fson P L
Biokhimiia. 1995 Nov;60(11):1903-10.
The binding of phosphorylase kinase to sarcoplasmic reticulum has been studied using gel chromatography. The presence of Ca2+, Mg2+ and glycogen was found to be necessary for the maximal binding. The phosphorylase kinase adsorbed on sarcoplasmic reticulum is capable of phosphorylating exogenous phosphorylase b. Phosphorylase kinase was shown to take no part in the phosphorylation of sarcoplasmic reticulum proteins. Exogenous calmodulin initiates the incorporation of [gamma-32P] of ATP into sarcoplasmic reticulum proteins. The data obtained point to a possibility that another Ca(2+)-calmodulin-dependent protein kinase may participate in the phosphorylation of sarcoplasmic proteins.
利用凝胶色谱法研究了磷酸化酶激酶与肌浆网的结合。发现Ca2+、Mg2+和糖原的存在是最大结合所必需的。吸附在肌浆网上的磷酸化酶激酶能够使外源性磷酸化酶b磷酸化。结果表明，磷酸化酶激酶不参与肌浆网蛋白的磷酸化。外源性钙调蛋白可启动ATP的[γ-32P]掺入肌浆网蛋白。所得数据表明，另一种Ca(2+)-钙调蛋白依赖性蛋白激酶可能参与肌浆蛋白的磷酸化。
