Separation of multiple forms of glutathione s-transferase from the blue mussel, mytilus edulis

P. J. Fitzpatrick, D. Sheehan

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

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.

Original languageBritish English
Pages (from-to)851-861
Number of pages11
JournalXenobiotica
Volume23
Issue number8
DOIs
StatePublished - 1993

Fingerprint

Dive into the research topics of 'Separation of multiple forms of glutathione s-transferase from the blue mussel, mytilus edulis'. Together they form a unique fingerprint.

Cite this