The isolation and characterization of the major glutathione S-transferase from the squid Loligo vulgaris

Add time:07/30/2019    Source:sciencedirect.com

1.1. 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 6.8.2.2. 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.3.3. The L. vulgaris GST did not cross-react with any of the available polyclonal antibodies raised against mammalian GSTs.4.4. Forty amino acids of its N-terminal sequence have been determined.5.5. Its activities and primary structure are compared with related proteins from other species.

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