The purification of the hepatic glutathione S-transferases of rainbow trout by glutathione affinity chromatography alters their isoelectric behaviour.
1. The basic glutathione S-transferases from rainbow-trout liver were more stable than the acidic ones. 2. The apparent pI values of these enzymes were lowered when they were eluted from a glutathione affinity column by reduced glutathione at pH 8.85. 3. The pI effect was not a function of the high pH alone, was diminished under conditions less favourable to glutathione oxidation, and did not occur when S-hexylglutathione affinity chromatography was used instead.
D000818:Animals; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005978:Glutathione; D005982:Glutathione Transferase / Q000302:isolation & purification*; D007526:Isoelectric Point; D008099:Liver / Q000201:enzymology*; D012487:Salmonidae / Q000378:metabolism*; D014337:Trout / Q000378:metabolism*
D005982:Glutathione Transferase; D005978:Glutathione