2. Academic Validation
  3. 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

  • Anal Biochem. 2008 Mar 1;374(1):25-30. doi: 10.1016/j.ab.2007.09.029.
Philip G Board 1,  Marjorie Coggan,  Jean Cappello,  Huina Zhou,  Aaron J Oakley,  M W Anders
Affiliations

Affiliation

  • 1 Molecular Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia. philip.board@anu.edu.au
PMID: 18028863 DOI: 10.1016/j.ab.2007.09.029
Abstract

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 1beta (IL-1beta). 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.

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