大鼠肝脏细胞核蛋白磷酸酶活性及其与细胞质蛋白磷酸酶的关系。

F Szeszák
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摘要

核蛋白磷酸酶(磷酸蛋白磷酸水解酶)3.1.3.16,缩写:NPPase)在不同条件下从大鼠肝细胞核和亚核部分中提取。NPPase活性被证明与染色质紧密结合,它的存在不能用细胞质从核制剂中不完全去除来解释。用乙醇或巯基乙醇处理后,NPPase的活化程度很小,这表明NPPase以其活化形式存在于细胞核中。另一方面,大鼠肝脏细胞质蛋白磷酸酶(简称:NPPase)经硫酸铵或乙醇沉淀后也仅表现出小程度的活化。因此,在兔肝脏和骨骼肌中观察到的胞质PPase的明显活化不能用于大鼠肝脏胞质和细胞核PPase的区分。
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Protein phosphatase activity in cell nuclei of rat liver and its relationship to the protein phosphatase in the cytoplasm.

Nuclear protein phosphatase (phosphoprotein phosphohydrolase, EC. 3.1.3.16, abbreviated: NPPase) was extracted from rat liver cell nuclei and subnuclear fractions under different conditions. NPPase activity proved to be strongly bound to chromatin and its presence cannot be explained by an incomplete removal of the cytoplasm from nuclear preparations. The small extent of activation of NPPase after treatment with ethanol or mercaptoethanol suggests that NPPase is present in the nucleus in its activated form. On the other hand, cytoplasmic protein phosphatase (abbreviated: NPPase) from rat liver also showed only a small extent of activation after precipitation with ammonium sulphate or ethanol. Therefore, the pronounced activation of cytoplasmic PPase, which has been observed in rabbit liver and skeletal muscle, cannot be used for differentiation between cytoplasmic and nuclear PPases in rat liver.

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