白色链霉菌中的蛋白质磷酸化

Protein phosphorylation in Streptomyces albus.

作者信息

Dobrová Z, Jiresová M, Petrík T, Rysavý P, Náprstek J, Janecek J

机构信息

Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.

出版信息

FEMS Microbiol Lett. 1990 Sep 1;59(1-2):145-8. doi: 10.1016/0378-1097(90)90047-t.

DOI:10.1016/0378-1097(90)90047-t

PMID:2276604

Abstract

The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in vivo. From cell extract which exhibited active phosphorylated in vitro, a protein kinase has been partially purified. The kinase activity was identified in fractions corresponding to a 90 kDa protein.

摘要

用[32P]正磷酸盐进行放射性标记的白色链霉菌磷酸化蛋白，已通过凝胶电泳和放射自显影进行了分析。发现有10多种蛋白质被磷酸化。以[32P]ATP为底物，无细胞提取物在体外使内源性蛋白质磷酸化，这些蛋白质在体内主要被磷酸化。从在体外表现出活性磷酸化的细胞提取物中，一种蛋白激酶已被部分纯化。在对应于90 kDa蛋白质的组分中鉴定出了激酶活性。