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盘基网柄菌AX-2菌株的蛋白激酶

Protein kinases of Dictyostelium discoideum, strain AX-2.

作者信息

Rahmsdorf H J, Pai S H

出版信息

Biochim Biophys Acta. 1979 Apr 12;567(2):339-46. doi: 10.1016/0005-2744(79)90120-7.

Abstract

In cell homogenates of Dictyostelium discoideum, strain AX-2, four major soluble protein kinases (ATP:protein phosphotransferase, EC 2.7.1.37) and one membrane-associated protein kinase activity were identified. The enzymes showed high affinity for casein. One of the enzymes was purified by affinity chromatography on casein-coated Sepharose. The soluble high molecular weight enzymes phosphorylated histones, whereas the low molecular weight enzymes did not. The same protein kinase species were present in vegetative and aggregation-competent cells. Their specific activity, however, changed during the development to aggregation competence. None of the enzymes was stimulated by cyclic AMP or cyclic GMP, regardless of their origin from vegetative or aggregation-competent cells.

摘要

在盘基网柄菌AX - 2菌株的细胞匀浆中,鉴定出了四种主要的可溶性蛋白激酶(ATP:蛋白质磷酸转移酶,EC 2.7.1.37)和一种与膜相关的蛋白激酶活性。这些酶对酪蛋白表现出高亲和力。其中一种酶通过在酪蛋白包被的琼脂糖上进行亲和层析得以纯化。可溶性高分子量酶能够磷酸化组蛋白,而低分子量酶则不能。在营养细胞和具备聚集能力的细胞中存在相同种类的蛋白激酶。然而,在发育至具备聚集能力的过程中,它们的比活性发生了变化。无论这些酶源自营养细胞还是具备聚集能力的细胞,均不受环磷酸腺苷(cAMP)或环磷酸鸟苷(cGMP)的刺激。

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