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

Abstract Glutathione-S-transferases (GSTs) are a family of Phase II detoxification enzymes
that catalyse the conjugation of glutathione (GSH) to a wide variety of endogenous and …

A remarkably diverse family of glutathione S-transferases (GSTs) has evolved in higher
organisms. These intracellular enzymes catalyze the nucleophilic attack of glutathione on a …

The glutathione S-transferases (GSTs) are a family of proteins that conjugate glutathione on
the sulfur atom of cysteine to various electrophiles (1-5). In addition, GST binds with high …

Adaptation and resistance to chemicals in the environment is a critical part of the
evolutionary process. As a result, a wide variety of defence systems that protect cells against …

SUMMARY A human colon cancer cell line with acquired multidrug resistance (MDR) was
assayed for the intracellular GSH level and the activity of GSH-S-transferase(GST), which …

In humans, the cytosolic glutathione S-transferase (GST) family of proteins is encoded by 16
genes presented in seven different classes. GSTs exhibit remarkable structural similarity …

The Glutathione S-transferases (GSTs) form a group of multi-gene isoenzymes involved in
the cellular detoxification of both xenobiotic and endobiotic compounds. GSTs have been …

The glutathione S-transferases (GSTs)'are a family of enzymes that catalyze the nucleophilic
addition of the thiol of reduced glutathione to a variety of electrophiles (1-9). In addition, the …

The super family of glutathione S-transferases (GSTs) is composed of multiple isozymes with
significant evidence of functional polymorphic variation. Over the last three decades, data …