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Separation of multiple forms of glutathione S -transferase from the Blue Mussel, Mytilus edulis

1993; Taylor & Francis; Volume: 23; Issue: 8 Linguagem: Inglês

10.3109/00498259309059413

1366-5928

Patrick Fitzpatrick, David Sheehan,

Pharmaceutical and Antibiotic Environmental Impacts

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.