Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors, and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes.
Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors, and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes.
复制标题
小牛肠道碱性磷酸酶、磷酸酶抑制剂和磷酸化化合物对糖皮质激素受体复合物激活率的影响。
DOI:
10.1021/bi00564a046
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发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
Litwack,G
中科院分区:
文献类型:
--
作者:
Barnett,CA;Schmidt,TJ;Litwack,G
Carol A. Barnett,*** § Thomas J. Schmidt, 5 and Gerald Litwack* abstract: The effects of (1) calf intestinal alkaline phosphatase,(2) phosphatase inhibitors, and (3) phosphorylated compounds on the rate of activation of rat liver and kidney glucocorticoid-receptor complexes have been investigated. The extent of activation has been quantitated by measuring the binding of [3H] triamcinolone acetonide-receptor complexes to DNA-cellulose and visualized by chromatographic sepa-ration of unactivated and activated 3H-labeled steroid-receptor complexes on DEAE-Sephadex A-50 or DEAE-cellulose. The addition of calf intestinal alkaline phosphatase stimulates the rate of activation (0 C, 2 h) of [3H] triamcinolone aceto-nide-receptor complexes in rat liver cytosol. Heat denaturation (90 C, 15 min) of the exogenous enzyme or addition of the competitive inhibitor, sodium arsenate, prevents the alkaline phosphatase mediatedstimulation. In addition, formation of activated [3H] triamcinolone acetonide-receptor complexes (25 C, 30 min) in rat liver and kidney cytosols is blocked by some phosphatase inhibitors (molybdate and tungstate) but not by