S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1

被引：43
|
作者：
Board, Philip G. [1 ]
Coggan, Marjorie [1 ]
Cappello, Jean [1 ]
Zhou, Huina [2 ]
Oakley, Aaron J. [2 ]
Anders, M. W. [3 ]
机构：
[1] Australian Natl Univ, John Curtin Sch Med Res, Mol Genet Grp, Canberra, ACT 2601, Australia
[2] Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia
[3] Univ Rochester, Med Ctr, Dept Physiol & Pharmacol, Rochester, NY 14642 USA
来源：
ANALYTICAL BIOCHEMISTRY | 2008年 / 374卷 / 01期
基金：
英国医学研究理事会;
关键词：
glutathione transferase omega 1-1; S-phenacylglutathione reductase; S-(4-nitrophenacyl)glutathione; enzyme activity;
D O I：
10.1016/j.ab.2007.09.029
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Glutathione transferase omega 1-1 (GSTO1-1) catalyzes the biotransformation of arsenic and is implicated as a factor influencing the age-at-onset of Alzheimer's disease and the posttranslational activation of interleukin 1 beta (IL-1 beta). Investigation of the biological role of GSTO1-1 variants has been hampered by the lack of a specific assay for GSTO1-1 activity in tissue samples that contain other GSTs and other enzymes with similar catalytic specificities. Previous studies (P. G. Board and M. W. Anders, Chem. Res. Toxicol. 20 (2007) 149-154) have shown that GSTO1-1 catalyzes the reduction of S-(phenacyl)glutathiones to acetophenones. A new substrate, S-(4-nitrophenacyl)glutathione (4NPG), has been prepared and found to have a high turnover with GSTO1-1 but negligible activity with GSTO2-2 and other members of the glutathione transferase superfamily. A spectrophotometric assay with 4NPG as a substrate has been used to determine GSTO1-1 activity in several human breast cancer cell lines and in mouse liver and brain tissues. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：25 / 30
页数：6
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