Separation of multiple forms of glutathione S-transferase from the blue mussel, Mytilus edulis.
1. Glutathione S-transferase isoenzymes from Mytilus edulis and M. galloprovincialis have been partially purified by glutathione-sepharose affinity chromatography followed by Mono Q anion exchange fast protein liquid chromatography (f.p.l.c.). 2. The tissue distribution of glutathione S-transferase in M. edulis has been studied. Using 1-chloro-2,4-dinitrobenzene as substrate, highest specific activity is observed in the gill, the main feeding organ. Affinity-purified extracts of this organ give a characteristic f.p.l.c. profile. A similar profile is obtained with affinity-purified extracts of the digestive gland of M. galloprovincialis. 3. The subunit structure of the purified isoenzymes has been studied by SDS polyacrylamide gel electrophoresis and reversed-phase h.p.l.c. The subunits have similar molecular weights and h.p.l.c. retention times to rat glutathione S-transferases.
Fitzpatrick
P J
PJ
Department of Biochemistry, University of College Cork, Mardyke, Ireland.
Sheehan
D
D
D000818:Animals; D049872:Bivalvia / Q000201:enzymology* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000096:biosynthesis; D005982:Glutathione Transferase / Q000302:isolation & purification*; D008658:Inactivation, Metabolic; D007527:Isoenzymes / Q000302:isolation & purification*; D015262:Xenobiotics / Q000493:pharmacokinetics
D007527:Isoenzymes; D015262:Xenobiotics; D005982:Glutathione Transferase; D005978:Glutathione