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- W2011149476 abstract "Abstract The cytosolic glutathione S-transferase from an Aedes albopictus cell line, C6/36, was sensitive to tetranitromethane, phenylglyoxal or pyridoxal phosphate modification, but was unaffected by N -acetylimidazole or diethyl pyrocarbonate. The extent of inactivation of the enzyme by those sensitive reagents was dependent on reagent concentrations but was biphasic in nature and did not follow pseudo-first-order kinetics. Glutathione, ethacrynic acid, S -(hexyl)glutathione, or S -(2,4-di-nitrophenyl)glutathione gave substantial protection of the enzyme from inactivation by these reagents. The modified enzyme showed varying Michaelis constants for glutathione ( K mGSH ) or 1-chloro-2,4-dinitrobenzene ( K mCDNB ) and a smaller catalytic constant ( k cat . These results indicate the involvement of tyrosine, arginine and lysine residues in the reaction mechanism of the mosquito C6/36 cell glutathione S-transferase. From the results of chemical modification and previous pH studies [Chang G.-G., Tsai L.-N., Tang S.-S., and Wang T.-C. (1994) Arch. Biochem. Biophys. 310, 134–143, we propose that tyrosine residue functions as a general base, promoting ionization of the thiol group of enzyme-bound glutathione and resulting in formation of a more reactive nucleophile thiolate that facilitates conjugation. The essential arginine and lysine residues may participate in maintenance of the correct active center structure." @default.
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- W2011149476 date "1995-05-01" @default.
- W2011149476 modified "2023-09-27" @default.
- W2011149476 title "Chemical modification of glutathione S-transferase from C6/36, an Aedes albopictus cell line" @default.
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- W2011149476 doi "https://doi.org/10.1016/0965-1748(94)00101-m" @default.
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