Effect of L-penicillamine hydantoin, an analogue of glutathione, on rat liver glutathione peroxidase, reductase and transferase reactions.

摘要: In soluble fractions prepared from rat liver homogenates, L-penicillamine hydantoin appeared to be, on the basis of SH consumption measurements, a substrate for glutathione peroxidase but not transferase reactions. When is incubated with proteins in presence penicillamine hydantoin, formation oxidized inhibited. Calculations Lineweaver-Burk plots point out that inhibition by peroxide-dependent oxidations mixed, since both apparent K(m) and V(max) values are modified. Preincubation led progressive inactivation peroxidase. The kinetics this process respect time inactivator concentration were studied. Inclusion preincubation mixture SH-containing molecules such as dithiothreitol, L-cysteine or protected enzyme against inactivation. However, none these neither Triton X-100, phenol, nor dialysis could reverse inactivated activated form. Mitochondrial was inhibited same extent its cytosolic counterpart. Modifications various subcellular markers enzymes (lactate dehydrogenase, N-acetyl beta-glucosaminidase, arylsulfatase C, butyryl-CoA lauryl-CoA glycolate oxidases) weak amplitude consisting either inhibition, stimulation.