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Evidence from heterologous expression of glutathione S-transferases A and A1 of the plaice (Pleuronectes platessa) that their endogenous role is in detoxification of lipid peroxidation products

Citation
Martinez-Lara E, Leaver M & George S (2002) Evidence from heterologous expression of glutathione S-transferases A and A1 of the plaice (Pleuronectes platessa) that their endogenous role is in detoxification of lipid peroxidation products, Marine Environmental Research, 54 (3-5), pp. 263-266.

Abstract
cDNA clones for glutathione S-transferases A (GST-A) and A1 (GST-A1) from plaice (Pleuronectes platessa) were expressed as N-terminally 6XHis tagged proteins in Escherichia coli and purified to homogeneity from Ni-NTA silica. GST-A was an efficient catalyst for conjugation of unsaturated alkenals derived from peroxidation of polyunsaturated fatty acids with the highest activity observed with trans-non-2-enal (8 μmol min-1 mg-1). GST-A1 was a very efficient Se-independent glutathione peroxidase with an activity towards cumene hydroperoxide of 25 μmol min-1 mg-1 . Although the enzymes exhibited moderately high activities towards the model substrate 1-chloro-2,4-dinitrobenzene (CDNB) they exhibited little or no activity towards other common prototypical xenobiotic substrates. Together with data for ontogeny, tissue distribution and inducibility of these enzymes, we contend that a primary function of these enzymes is protection from the harmful effects of lipid peroxidation products generated naturally or exacerbated by xenobiotic exposure.

Keywords
plaice; glutathione-S-transferase; lipid oxidation

StatusPublished
AuthorsMartinez-Lara Esther, Leaver Michael, George Stephen
Publication date09/2002
Publication date online28/05/2002
URLhttp://www.sciencedirect.com/…0141113602001885
PublisherElsevier
ISSN 0141-1136
LanguageEnglish

Journal
Marine Environmental Research: Volume 54, Issue 3-5 (SEP-DEC 2002)

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