Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase.
Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase.
复制标题
内源性蛋白激酶对大鼠肝脏中纯化的糖皮质激素受体进行磷酸化。
DOI：
10.1016/s0006-291x(84)80307-1
复制
发表时间：
1984
影响因子：
3.1
通讯作者：
Jacob,ST
中科院分区：
文献类型：
--
作者：
Kurl,RN;Jacob,ST
用地塞米松亲和柱从大鼠肝胞液中纯化糖皮质激素受体。如此纯化的受体在SDS-聚丙烯酰胺凝胶电泳时显示单一的蛋白质条带。其分子量为90，000，与其他糖皮质激素受体制剂的报告值一致。用[ρ 32 P] ATP和Mg 2+孵育纯化的制备物导致[32 P]转移到受体蛋白，表明存在能够磷酸化受体分子的内源性蛋白激酶活性。内源性蛋白激酶对糖皮质激素受体的磷酸化可能是该受体活化的直接机制。
Glucocorticoid receptor was purified from rat liver cytosol using a dexamethasone affinity column. The receptor thus purified displayed a single protein band when subjected to SDS-polyacrylamide gel electrophoresis. It had a molecular weight of 90,000 which was consistent with the reported value for other glucocorticoid receptor preparations. Incubation of the purified preparation with [ρ32P] ATP and Mg2+resulted in transfer of [32P] to the receptor protein indicating the presence of an endogeneous protein kinase activity capable of phosphorylating the receptor molecule. Phosphorylation of the glucocorticoid receptor by the endogenous protein kinase might serve as a direct mechanism for the activation of the receptor.