Abstract
Glutathione 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.
Keywords: Glutathione transferase, An. cracens, Epsilon class, 4-HNE, lipid peroxidation, oxidative stress
Protein & Peptide Letters
Title: Molecular Cloning and Expression of Several New Anopheles cracens Epsilon Class Glutathione Transferases
Volume: 16 Issue: 1
Author(s): Jeerang Wongtraku, Jantana Wongsantichon, Ardcharaporn Vararattanavech, Posri Leelapat, La-aied Prapanthadara and Albert J. Ketterman
Affiliation:
Keywords: Glutathione transferase, An. cracens, Epsilon class, 4-HNE, lipid peroxidation, oxidative stress
Abstract: Glutathione 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.
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Cite this article as:
Wongtraku Jeerang, Wongsantichon Jantana, Vararattanavech Ardcharaporn, Leelapat Posri, Prapanthadara La-aied and Ketterman J. Albert, Molecular Cloning and Expression of Several New Anopheles cracens Epsilon Class Glutathione Transferases, Protein & Peptide Letters 2009; 16 (1) . https://dx.doi.org/10.2174/092986609787049367
DOI https://dx.doi.org/10.2174/092986609787049367 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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