The isolation and characterization of the major glutathione S-transferase from the squid Loligo vulgaris.
1. The major glutathione S-transferase (GST) from the common squid Loligo vulgaris has been purified and shown to be a homodimer of subunit molecular mass 24,000 and pI 6.8. 2. It has high activity towards 1-chloro-2,4-dinitrobenzene, p-nitrobenzyl chloride, 4-hydroxynon-2-enal and linoleic acid hydroperoxide, low activity with 1,2-dichloro-4-nitrobenzene and no activity with ethacrynic acid, trans-4-phenyl-3-buten-2-one and 1,2-epoxy-3-(p-nitrophenoxy)propane. 3. The L. vulgaris GST did not cross-react with any of the available polyclonal antibodies raised against mammalian GSTs. 4. Forty amino acids of its N-terminal sequence have been determined. 5. Its activities and primary structure are compared with related proteins from other species.
Harris
J
J
Department of Biochemistry, University College and Middlesex School of Medicine, London, UK.
Coles
B
B
Meyer
D J
DJ
Ketterer
B
B
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D049832:Decapodiformes / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015151:Immunoblotting; D007526:Isoelectric Point; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity
D007527:Isoenzymes; D046911:Macromolecular Substances; D005982:Glutathione Transferase