[A comparative study of the substrate and inhibitor specificity of the glutathione transferase from the spring grain aphid (Schizaphis gramina Rond.) and from rat liver].

Kinetic parameters of 9 substrates interaction with glutathione transferase (GST) from spring grain aphid and rat were studied. The most significant difference in Vmax values was noticed for 4-nitropyridine-N-oxide (6 times higher for aphid) and ethacrynic acid (7 times higher for rat). Km values were practically in all cases higher for aphid GST as compared to rat GST.

[Selective N-heterylazimine inhibition of reactions catalyzed by rat liver glutathione transferase].

Three reactions (nucleophile substitution, thiolysis and N-deoxygenation) catalyzed by rat liver glutathione transferase have been studied using several N-heterylazimine inhibitors. The inhibitors are sharply different in their effectiveness in the transferase reactions. Their efficiency depends on their structure.

[Interaction of the rat liver glutathione transferase system with 1-phthalimidoazimines].

The interaction of rat liver glutathione and glutathione transferase with several 1-phthalimidoazimines is studied. Differences between spontaneous and enzymatic reactions of azimines and reduced glutathione are shown. It is pointed out that the formation of glutathione-azimine complexes takes place in the reaction mixture.