从未成熟大鼠子宫的磷酸蛋白磷酸酶活性中分离“雌激素诱导”蛋白。
Separation of "estrogen-induced" protein from phosphoprotein phosphatase activity of immature rat uterus.
作者信息
Kaye A M, Walker M D, Sömjen D
出版信息
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2631-4. doi: 10.1073/pnas.72.7.2631.
Preparations of the "induced protein" which appears in the rat uterus within 40 min of estradiol administration have recently been reported to contain phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activity. We found that these two proteins distribute differently on ammonium sulfate fractionation of uterine cytosol. Preparative cellulose acetate electrophoresis afforded complete (greater than 99.9%) separation of phosphoprotein phosphatase activity from the induced protein. The specific activity of phosphoprotein phosphatase in uterine cytosol was unchanged 1, 4, 12, or 24 hr after estradiol administration. These results are incompatible with the view that the induced protein mediates estrogen action by virtue of an inherent phosphoprotein phosphatase activity.
据报道，在给予雌二醇后40分钟内出现在大鼠子宫中的“诱导蛋白”制剂含有磷酸蛋白磷酸酶（磷酸蛋白磷酸水解酶，EC 3.1.3.16）活性。我们发现，这两种蛋白质在子宫细胞溶质的硫酸铵分级分离中分布不同。制备性醋酸纤维素电泳可将磷酸蛋白磷酸酶活性与诱导蛋白完全（大于99.9%）分离。给予雌二醇后1、4、12或24小时，子宫细胞溶质中磷酸蛋白磷酸酶的比活性没有变化。这些结果与诱导蛋白凭借内在的磷酸蛋白磷酸酶活性介导雌激素作用的观点不一致。
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