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Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/7631

Appears in Collections:Aquaculture Journal Articles
Peer Review Status: Refereed
Title: A piscine glutathione S-transferase which efficiently conjugates the end- products of lipid peroxidation
Author(s): Leaver, Michael
George, Stephen
Contact Email: m.j.leaver@stir.ac.uk
Issue Date: Jul-1998
Publisher: Elsevier
Citation: Leaver M & George S (1998) A piscine glutathione S-transferase which efficiently conjugates the end-products of lipid peroxidation, Marine Environmental Research, 46 (1-5), pp. 71-74.
Abstract: A cDNA clone for glutathione S-transferaseA (GSTA) from plaice (Pleuronectes platessa) was expressed in Eschericia coli (E. coli) and purified to homogeneity by S-hexylglutathione affinity chromatography. When compared to literature values for a variety of purified mammalian GSTs, the heterologously expressed purified plaice enzyme had moderate activity towards the model substrate 1,2- chloro-2,4-dinitrobenzene (CDNB) and exhibited a Km of 2.5 ± 2 mM and Vmax of 30.9 ± 2.3 μmol min-1 mg-1. It had little or no activity towards several other model GST substrates including 1,2-dinitrochloro-4-benzene (DCNB), ethacrynic acid (EA), and p-nitrobenzylchloride (NBC). However plaice GSTA was a relatively efficient catalyst for the conjugation of a series of alk-2-enals and alk-2,4- dienals and also 4-hydroxynonenal. The highest activity observed with this series of substrates was with trans-non-2-enal with a Km of 17.9 ± 2.2 μM and a Vmax of 3.01 ± 0.57 μmol min-1 mg-1. These unsaturated alkenals have been identified in cells and cell extracts as highly toxic products arising from peroxidation of unsaturated fatty acids particularly during periods of oxidative stress. Fish are relatively rich in polyunsaturated fatty acids and thus GSTA mediated conjugation may be an important mechanism for detoxifying peroxidised lipid breakdown pr
Type: Journal Article
URI: http://hdl.handle.net/1893/7631
URL: http://www.sciencedirect.com/science/article/pii/S0141113697000718
DOI Link: http://dx.doi.org/10.1016/S0141-1136(97)00071-8
Rights: The publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.
Affiliation: Aquaculture
Aquaculture

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