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• W2037873257 abstract "The glutathione S-transferases (GST) are a supergene family of phase II detoxification enzymes which catalyse the S-conjugation between glutathione and an electrophilic substrate. The active site can be divided into two adjacent functional regions, a highly specific G-site for binding the physiological substrate glutathione and a nonspecific H-site for binding nonpolar electrophilic substrates. Equilibrium and kinetic unfolding experiments employing tryptophan fluorescence and enzyme activity measurements were performed to study the effect of ligand binding to the G-site on the unfolding and stability of the porcine class pi glutathione S-transferase against urea. The presence of glutathione caused a shift in the equilibrium-unfolding curves towards lower urea concentrations and enhanced the first-order rate constant for unfolding suggesting a destabilisation of the pGSTP1-1 structure against urea. The presence of either glutathione sulphonate or S-hexylglutathione, however, produced the opposite effect in that their binding to the G-site appeared to exert a stabilising effect against urea. The binding of these glutathione analogues also reduced significantly the degree of cooperativity of unfolding indicating a possible change in the protein's unfolding pathway." @default.
• W2037873257 created "2016-06-24" @default.
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• W2037873257 date "1996-08-12" @default.
• W2037873257 modified "2023-10-18" @default.
• W2037873257 title "Effect of glutathione, glutathione sulphonate and S-hexylglutathione on the conformational stability of class pi glutathione S-transferase" @default.
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• W2037873257 doi "https://doi.org/10.1016/0014-5793(96)00768-5" @default.
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