title: The major rat heart glutathione S-transferases are anionic isozymes composed of Yb size subunits.
abstract: The GSH S-transferases from rat heart cytosol has been purified by S-hexylglutathione-linked Sepharose-6B affinity chromatography. The majority (approximately 80%) of these GSH S-transferases are anionic isozymes which can be resolved further by DEAE-cellulose column chromatography and isoelectric focusing. They are mainly composed of Yb size (Mr = 27,000) subunits with different substrate specificity patterns from the rat liver anionic GSH S-transferases. The major cationic GSH S-transferases from liver are not expressed in rat heart. Although some cationic GSH S-transferases from rat heart can be purified by CM-cellulose column chromatography they are composed of major subunits of Yb electrophoretic mobility.
mesh_terms: D000375:Aging; D000818:Animals; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism; D006321:Heart / Q000254:growth & development; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D046911:Macromolecular Substances; D005982:Glutathione Transferase