Strain- and sex-specific differences in the glutathione S-transferase class pi in the mouse examined by gradient elution of the glutathione-affinity matrix and reverse-phase high performance liquid chromatography

• Published in: Biochimica et biophysica acta. General subjects Vol. 1243; no. 2; pp. 256 - 264
• Main Authors: Egaas, Eliann, Falls, J.Greg, Svendsen, Nina O, Ramstad, Hanne, Skaare, Janneche U, Dauterman, Walter C
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 23.02.1995
• ISSN: 0304-4165; 1872-8006
• DOI: 10.1016/0304-4165(94)00138-N

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.