Abstract
The cationic glutathione S-transferase (GST σ) of human erythrocytes is activated when incubated with 1 mM N-ethylmaleimide or other sulfhydryl blocking agents. Other GST isoenzymes of human tissues were inhibited by these reagents under similar conditions. At higher concentrations of NEM, GST σ was also inhibited. Dithiothreitol, 2-mercaptoethanol, and sodium borohydride also caused several fold activation of GST σ but none of the other human GST isoenzymes were activated by these reagents.
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