http://hdl.handle.net/1893/7615
Appears in Collections: | Aquaculture Journal Articles |
Peer Review Status: | Refereed |
Title: | 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 |
Author(s): | Martinez-Lara, Esther Leaver, Michael George, Stephen |
Contact Email: | m.j.leaver@stir.ac.uk |
Keywords: | plaice glutathione-S-transferase lipid oxidation |
Issue Date: | Sep-2002 |
Date Deposited: | 24-Aug-2012 |
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. http://www.sciencedirect.com/science/article/pii/S0141113602001885; https://doi.org/10.1016/S0141-1136%2802%2900188-5 |
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. |
URL: | http://www.sciencedirect.com/science/article/pii/S0141113602001885 |
DOI Link: | 10.1016/S0141-1136(02)00188-5 |
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