ISOLATION, PROPERTIES AND INDUCTION OF PLAICE LIVER CYTOSOLIC GLUTATIONE-S-TRANSFERASES

Three cytosolic glutathione S-transferases [E.C. 2.5.1.18] were identified in liver of a marine flatfish, the plaice (Pleuronectes platessa) and the two major isoforms were purified to homogeneity. There was no evidence for the presence of basic transferases. The plaice GST's exhibited comparable hematin binding to rat ligandin, however, bilirubin was only bound weakly and the enzymes did not display the inhibition characteristics of ligandin. They were extremely sensitive to inhibition by organotin compounds. Plaice transferase A was a homodimer of Mr 27 kDa subunits; it displayed strongest activity with CDNB and some activity with DCNB as substrates. Specific antibodies to it did not show any relationship with other plaice GST's or rat GST subunits 1,2,3,4,7,8 or 10. Plaice transferase B was a homodimer of Mr 25 kDa subunits, it displayed similar activities with CDNB and DCNB as substrates to transferase A and a low activity with ethacrynic acid or p-nitrobenzylchloride. It was immunologically related to the rat alpha class transferase subunits 1,2 and 8. A minor form, transferase AM, which was not separated from transferase A, appeared to be a heterodimer of Mr 25.5 and 27 kDa subunits. It displayed a greater activity with DCNB than the other plaice GST's and some activity with bromosulphalein indicative of a possible relationship with the Mu class transferases. © 1990 Kugler Publications.