S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1
S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1
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DOI:
10.1016/j.ab.2007.09.029
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发表时间:
2008-03-01
影响因子:
2.9
通讯作者:
Anders, M. W.
中科院分区:
文献类型:
--
作者:
Board, Philip G.;Coggan, Marjorie;Anders, M. W.
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.