纤细裸藻Z株精氨酸：单ADP - 核糖水解酶的纯化与特性分析

Purification and characterization of arginine:mono-ADP-ribosylhydrolase from Euglena gracilis Z.

作者信息

Takenaka S, Masuda W, Tsuyama S, Tamura Y, Miyatake K, Nakano Y

机构信息

Department of Applied Biological Chemistry, Osaka Prefecture University.

出版信息

J Biochem. 1996 Oct;120(4):792-6. doi: 10.1093/oxfordjournals.jbchem.a021481.

DOI:10.1093/oxfordjournals.jbchem.a021481

PMID:8947843

Abstract

Arginine:mono-ADP-ribosylhydrolase was purified from a protozoan, Euglena gracilis Z, using [32P]mono-ADP-ribosylated actin as a substrate. The enzyme showed molecular mass of 33 kDa both in SDS PAGE and gel filtration, indicating it to be a monomeric protein. It was strongly inhibited by ADP and ADP-ribose and activated by Mg2+, DTT, and 2-mercaptoethanol. These results suggest that it recognizes the ADP-ribose moiety of the modified protein. Since the enzyme activity increased in S phase and late G0 phase in a synchronous dividing culture, the enzyme may function in the regulation of the cell cycle.

摘要

精氨酸

单磷酸腺苷 - 核糖水解酶是从原生动物纤细裸藻（Euglena gracilis Z）中纯化得到的，使用[32P]单磷酸腺苷 - 核糖基化的肌动蛋白作为底物。该酶在SDS - PAGE和凝胶过滤中均显示分子量为33 kDa，表明它是一种单体蛋白。它受到ADP和ADP - 核糖的强烈抑制，并被Mg2 +、DTT和2 - 巯基乙醇激活。这些结果表明它能识别修饰蛋白的ADP - 核糖部分。由于在同步分裂培养中，该酶活性在S期和G0晚期增加，因此该酶可能在细胞周期调控中发挥作用。