Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/7631
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dc.contributor.authorLeaver, Michaelen_UK
dc.contributor.authorGeorge, Stephenen_UK
dc.date.accessioned2012-08-27T08:13:06Z-
dc.date.available2012-08-27T08:13:06Zen_UK
dc.date.issued1998-07en_UK
dc.identifier.urihttp://hdl.handle.net/1893/7631-
dc.description.abstractA 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 products.en_UK
dc.language.isoenen_UK
dc.publisherElsevieren_UK
dc.relationLeaver 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. http://www.sciencedirect.com/science/article/pii/S0141113697000718; https://doi.org/10.1016/S0141-1136%2897%2900071-8.en_UK
dc.rightsThe 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.en_UK
dc.titleA piscine glutathione S-transferase which efficiently conjugates the end-products of lipid peroxidationen_UK
dc.typeJournal Articleen_UK
dc.rights.embargodate2999-01-01en_UK
dc.rights.embargoreason[1-s2.0-S0141113697000718-main.pdf] : The publisher does not allow this work to be made publicly available in this Repository therefore there is an embargo on the full text of the work.en_UK
dc.identifier.doi10.1016/S0141-1136(97)00071-8en_UK
dc.citation.jtitleMarine Environmental Researchen_UK
dc.citation.issn0141-1136en_UK
dc.citation.volume46en_UK
dc.citation.issue1-5en_UK
dc.citation.spage71en_UK
dc.citation.epage74en_UK
dc.citation.publicationstatusPublisheden_UK
dc.citation.peerreviewedRefereeden_UK
dc.type.statusVoR - Version of Recorden_UK
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S0141113697000718en_UK
dc.author.emailm.j.leaver@stir.ac.uken_UK
dc.citation.date28/06/1999en_UK
dc.contributor.affiliationInstitute of Aquacultureen_UK
dc.contributor.affiliationInstitute of Aquacultureen_UK
dc.identifier.isi000075806100017en_UK
dc.identifier.scopusid2-s2.0-0032122371en_UK
dc.identifier.wtid791896en_UK
dc.contributor.orcid0000-0002-3155-0844en_UK
dc.date.firstcompliantdepositdate2012-08-24en_UK
Appears in Collections:Aquaculture Journal Articles

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