The glutathione S-transferases (GST) represent a major group of detoxification enzymes. All
eukaryotic species possess multiple cytosolic and membrane-bound GST isoenzymes, each …

The glutathione transferases (EC 2.5. 1.18) are known as enzymes that catalyze the
nucleophilic attack of the sulfur atom of glutathione on electrophilic groups in a second …

The glutathione S-transferase (GST) supergene family comprises gene families that encode
isoenzymes that are widely expressed in mammalian tissue cytosols and membranes. Both …

Glutathione (GSH) alone detoxifies electrophiles with an effectiveness which depends on
the rate of the reaction and the concentration of GSH. If electrophiles are substrates for GSH …

The glutathione transferases, a family of multifunctional proteins, catalyze the glutathione
conjugation reaction with electrophilic compounds biotransformed from xenobiotics …

The importance of the covalent binding of electrophilic metabolites of carcinogens to
macromolecules, in particular DNA, as a critical event in chemical carcinogenesis was …

Publisher Summary This chapter focuses on the biomedical applications of ubiquitous and
modest size enzymes, glutathione S-transferases (GST), found in bacteria, yeast …

Human glutathione transferases (GSTs) are a multigene family of enzymes that are involved
in the metabolism of a wide range of electrophilic compounds of both exogenous and …

The regulation of glutathione and various glutathione-dependent enzymes has been studied
in two ovarian adenocarcinoma cell lines derived from a patient before (PE01) and after …

The glutathione transferases (GSTs) are involved in the metabolism of a wide range of
compounds of both exogenous and endogenous origin. There is evidence that deficiency of …