Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein

被引：36

作者：

Winstall, E

Affar, EB

Shah, R

Bourassa, S

Scovassi, AI

Poirier, GG

机构：

[1] Univ Laval, CHUQ, CHUL Res Ctr, Hlth & Environm Unit, Ste Foy, PQ G1V 4G2, Canada

[2] CNR, Ist Genet Biochim & Evoluzionist, I-27100 Pavia, Italy

来源：

EXPERIMENTAL CELL RESEARCH | 1999年 / 246卷 / 02期

基金：

英国医学研究理事会;

关键词：

poly(ADP-ribose) glycohydrolase; posttranslational modification; DNA damage; poly(ADP-ribose) polymerase;

D O I：

10.1006/excr.1998.4321

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. Purification of PARG from many tissues revealed heterogeneity in activity and structure of this enzyme. To investigate PARG structure and localization, we developed a highly sensitive one-dimensional zymogram allowing us to analyze PARG activity in crude extracts of Cos-7, Jurkat, HL-60, and Molt-3 cells. In all extracts, a single PARG activity band corresponding to a protein of about 110 kDa was detected. This 110-kDa PARG activity was found mainly in cytoplasmic rather than in nuclear extracts Of Cos-7 cells. (C) 1999 Academic Press.

引用

页码：395 / 398

页数：4

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