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dc.contributor.authorJeerang Wongtrakulen_US
dc.contributor.authorJantana Wongsantichonen_US
dc.contributor.authorArdcharaporn Vararattanavechen_US
dc.contributor.authorPosri Leelapaten_US
dc.contributor.authorLa Aied Prapanthadaraen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.date.accessioned2018-09-10T03:14:49Z-
dc.date.available2018-09-10T03:14:49Z-
dc.date.issued2009-01-01en_US
dc.identifier.issn09298665en_US
dc.identifier.other2-s2.0-61549105346en_US
dc.identifier.other10.2174/092986609787049367en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=61549105346&origin=inwarden_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/59409-
dc.description.abstractGlutathione transferases, GSTs, are detoxification proteins that are found in most organisms. The acGSTE3-3 had the ability to conjugate 4-hydroxynonenal, a cytotoxic lipid peroxidation product. Although other Epsilon GSTs showed roles in insecticide metabolism, the acGSTE3-3 appeared to have a major role in detoxifying lipid peroxidation products conferring protection against oxidative damage. © 2009 Bentham Science Publishers Ltd.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleMolecular cloning and expression of several new anopheles cracens epsilon class glutathione transferasesen_US
dc.typeJournalen_US
article.title.sourcetitleProtein and Peptide Lettersen_US
article.volume16en_US
article.stream.affiliationsChiang Mai Universityen_US
article.stream.affiliationsMahidol Universityen_US
Appears in Collections:CMUL: Journal Articles

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