Abstract
Glutathione S-transferase (GST) isoenzymes isolated from human tissues and rat liver are differentially inhibited by quercetin, alizarin, purpurogallin and ellagic acid. Rat liver GST isoenzymes are far more sensitive to these compounds as compared to the human GST isoenzymes. Among human GST, the anionic isoenzymes containing C type and A' type subunits are inhibited to a greater extent as compared to the cationic isoenzymes containing A and B type subunits. The anionic GST isoenzymes of human erythrocytes and placenta are differentially inhibited by these plant phenols indicating that the placental and erythrocyte isoenzymes may be distinct proteins.
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