来自HeLa细胞核的与hnRNP相关的蛋白激酶。部分纯化及特性

Protein kinase associated with hnRNP from Hela cell nuclei. Partial purification and properties.

作者信息

Periasamy M, Brunel C, Jeanteur P

出版信息

Biochimie. 1979;61(7):823-6. doi: 10.1016/s0300-9084(79)80276-x.

Abstract

The protein kinase previously described as an endogenous activity present in ribonucleoprotein particles containing heterogenous RNA from HeLa cells (Blanchard et al, Eur. J. Biochem (1977), 79, 11-131) has been partially purified by a combination of chromatography on DEAE cellulose, phosphocellulose and Sephacryl S-200. It is able to phosphorylate exogenous substrates, among which casein is the most efficient. Its enzymatic properties were found to be quite similar to those described for the endogenous activity. Its activity is independent of cyclic AMP as well as of the calcium-dependent regulator protein and is inhibited by hemin. Its native molecular weight is around 48,000 as determined by gel filtration.

摘要

先前被描述为存在于含有来自HeLa细胞的异源RNA的核糖核蛋白颗粒中的一种内源性活性的蛋白激酶（Blanchard等人，《欧洲生物化学杂志》（1977年），79卷，11 - 131页），已通过在DEAE纤维素、磷酸纤维素和Sephacryl S - 200上的色谱法组合进行了部分纯化。它能够磷酸化外源底物，其中酪蛋白是最有效的。发现其酶学性质与所描述的内源性活性的性质非常相似。其活性不依赖于环磷酸腺苷以及钙依赖性调节蛋白，并且被血红素抑制。通过凝胶过滤测定，其天然分子量约为48,000。