Phosphorylation in vivo of rat hepatic glucocorticoid receptor.
Phosphorylation in vivo of rat hepatic glucocorticoid receptor.
复制标题
大鼠肝糖皮质激素受体的体内磷酸化。
DOI：
10.1016/0006-291x(84)91413-x
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发表时间：
1984
影响因子：
3.1
通讯作者：
Litwack,G
中科院分区：
文献类型：
--
作者：
Grandics,P;Miller,A;Schmidt,TJ;Litwack,G
用[~（32）P]正磷酸标记大鼠肝糖皮质激素受体。在最后两个分级程序中，得到纯化的、双氢叶酸盐稳定的、未活化的受体复合物，结合的[32 P]与结合的[3 H]曲安奈德峰共洗脱。SDS凝胶电泳显示[32 P]标记的90 K和24 K带。较低分子量条带严重磷酸化，可能是未活化受体的组分或降解产物。
Rat liver glucocorticoid receptors were labeled in vivo with [32 P] orthophosphate. In the last two fractionation procedures leading to purified, molybdate-stabilized, unactivated receptor complex, bound [32 P] coeluted with peaks of bound [3 H] triamcinolone acetonide. SDS-gel electrophoresis revealed [32 P] labeled 90K and 24K bands. The lower molecular weight band is heavily phosphorylated and it could be either a component of the unactivated receptor or a degradation product.