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- W1973587765 abstract "Saligenin cyclic phosphates (SCPs) are activated as a glutathione transferase (GSH-t) inhibitor, i.e., S-(2-hydroxybenzyl)glutathione, by conjugation with glutathione (GSH). However, another type of inhibition of GSH-t activity was observed by SCPs in the absence of GSH and it proceeded in a time-dependent manner. The enzyme that was inhibited by K-2, one of the SCPs, was not reactivated by gel filtration in contrast to the enzyme inhibited by S-(2-hydroxybenzyl)glutathione which was almost completely reactivated by gel filtration. The enzyme was radiolabeled after incubation with [ring-14C]salioxon, one of the SCPs, under physiological conditions. In experiments using reagents to modify specific amino acid residues, cysteine was found to be the most important one in GSH-t activity, but histidine also contributed to the activity. Equine liver GSH-t which was inhibited by K-2 did not react with a thiol-specific fluorescent probe, whereas the active enzyme was labeled with the fluorophore. These results suggest that SCPs irreversibly inactivate GSH-t probably by 2-hydroxybenzylation on a cysteine residue." @default.
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- W1973587765 date "1992-02-01" @default.
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- W1973587765 title "Irreversible inactivation of glutathione transferases by saligenin cyclic phosphates" @default.
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- W1973587765 doi "https://doi.org/10.1016/0048-3575(92)90059-9" @default.
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