Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
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.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
article.title.sourcetitleProtein and Peptide Lettersen_US
article.volume16en_US Mai Universityen_US Universityen_US
Appears in Collections:CMUL: Journal Articles

Files in This Item:
There are no files associated with this item.

Items in CMUIR are protected by copyright, with all rights reserved, unless otherwise indicated.