Activation of the rat liver glucocorticoid--receptor complex.
Activation of the rat liver glucocorticoid--receptor complex.
复制标题
大鼠肝脏糖皮质激素受体复合物的激活。
DOI：
10.1021/bi00629a012
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发表时间：
1977
期刊：
影响因子：
2.9
通讯作者：
G. Litwack
中科院分区：
文献类型：
--
作者：
J. Goidl;M. Cake;K. Dolan;L. Parchman;G. Litwack
大鼠肝脏糖皮质激素受体通过三种程序被激活：加热、凝胶过滤和稀释。随着热激活后的时间，类固醇受体复合体失去了与DNA-纤维素结合的能力，而被Sephadex G-25激活并经稀释后的受体保持了与DNA-纤维素的结合能力。激活型和非激活型受体的激素解离率基本相同。然而，未激活的受体能够与类固醇重新结合，而激活的受体对类固醇的重新结合能力降低。凝胶过滤和稀释实验结果表明，大鼠肝细胞浆中存在一种参与活化过程的低分子因子(S)。
The rat liver glucorcorticoid receptor has been activated using three procedures: heat, gel filtration, and dilution. With time after heat activation the steroid--receptor complex loses its capacity to bind to DNA--cellulose, while receptor activated by Sephadex G-25 and by dilution maintains DNA--cellulose binding capacity. The rates of steroid dissociation from nonactivated and activated receptor and essentially identical. However, nonactivated receptor is capable of rebinding steroid, while activated receptor has a reduced capacity to rebind steroid. The results of the gel filtration and dilution studies suggest that a low-molecular-weight factor(s) exists in rat liver cytosol which is involved in the process of activation.