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dc.contributor.authorJeerang Wongtrakulen_US
dc.contributor.authorSaengtong Pongjaroenkiten_US
dc.contributor.authorPosri Leelapaten_US
dc.contributor.authorWoottichai Nachaiwiengen_US
dc.contributor.authorLa Aied Prapanthadaraen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.description.abstractGlutathione transferases (GSTs) (E.C. are multifunctional enzymes involved in the detoxification of many exogenous and endogenous compounds. This study aimed to characterize several new GSTs from Anopheles cracens, a major Thai malaria vector formerly known as Anopheles dirus. The three recombinant enzymes obtained were from the epsilon, theta and omega classes. They showed 8093% identity to orthologous An. gambiae GSTs. AcGSTE2-2 possessed peroxidase activity that cannot be detected for the An. gambiae AgGSTE2-2. AcGSTT1-1 had high activity toward several substrates that are specific for mammalian theta class. The AcGSTO1-1 can use 1-chloro-2,4-dinitrobenzene, dichloroacetic acid, and hydroxyethyl disulfide substrates. The enzymes bound but did not metabolize the organophosphate temephos. The epsilon AcGSTE2-2 functioned as a peroxidase and DDT metabolizing enzyme. The theta AcGSTT1-1 functioned not only as peroxidase but also acted as a binding protein for organophosphates. The omega GST had thiol transferase activity suggesting a role in oxidative stress response. © 2010 Entomological Society of America.en_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleExpression and characterization of three new glutathione transferases, an epsilon (AcGSTE2-2), Omega (AcGSTO1-1), and Theta (AcGSTT1-1) from anopheles cracens (Diptera: Culicidae), a major thai malaria vectoren_US
article.title.sourcetitleJournal of Medical Entomologyen_US
article.volume47en_US Mai Universityen_US Universityen_US Universityen_US
Appears in Collections:CMUL: Journal Articles

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