A gradient elution with glutathione (GSH) from a GSH-Sepharose 6B affinity column separated the hepatic mouse glutathione S-transferases (GST) to the alpha-, mu- and pi-classes. The GST-dependent conjugation of atrazine and glutathione was catalyzed by a pi-class GST. The pi- and mu-classes were both identified by their respective specific substrates, and after reverse-phase HPLC, by N-terminal analysis of 19-35 of the amino acids. The alpha-class GST was associated with a high selenium-independent GSH peroxidase activity and the purified protein had a N-blocked terminal. Strain related differences in the pi-class GST of the CD-1, C57BL/6, DBA/2 and Swiss-Webster males were observed by PhastGel electrophoresis of the GSH affinity chromatograph separated fractions, reverse phase HPLC and by N-terminal amino acid sequence analysis.
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