Conjugation of acrylamide with glutathione catalysed by glutathione-S-transferases of rat liver and brain

Abstract

Acrylamide, an α , β unsaturated electrophile and a cumulative neurotoxin, was found to react with glutathione giving rise to an S-conjugate of acrylamide. Glutathione S-transferase of rat liver and brain cytosols (active on both acrylamide and 1-chloro 2,4 dinitrobenzene) emerged as a single major peak on elution from Sephadex G-75. The enzymic conjugation of acrylamide with glutathione increased with protein and was dependent on incubation time and pH of medium. Acrylamide inhibited glutathione-S-transferase activity towards 1-chloro 2,4-dinitro-benzene of both liver and brain cytosol, in a concentration and time dependent manner. Enzyme catalyzed conjugation of acrylamide with glutathione was induced significantly by phenobarbital and t-SO (tans-stilbene oxide). The enzymic conjugation of acrylamide increased two fold from neonatal to adult and then showed a decreasing pattern at subsequent ages.