Publication: Expression and characterization of a novel class of glutathione S-transferase from Anopheles dirus
Issued Date
2002-03-21
Resource Type
ISSN
09651748
Other identifier(s)
2-s2.0-0036009123
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Insect Biochemistry and Molecular Biology. Vol.32, No.4 (2002), 425-433
Suggested Citation
R. Udomsinprasert, A. J. Ketterman Expression and characterization of a novel class of glutathione S-transferase from Anopheles dirus. Insect Biochemistry and Molecular Biology. Vol.32, No.4 (2002), 425-433. doi:10.1016/S0965-1748(01)00119-9 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/19985
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Expression and characterization of a novel class of glutathione S-transferase from Anopheles dirus
Author(s)
Other Contributor(s)
Abstract
A new Anopheles dirus glutathione S-transferase (GST) has been obtained and named adGST4-1. Both genomic DNA and cDNA for heterologous expression were acquired. The genomic sequence was 3188 bp and consisted of the GST gene as well as flanking sequence. The flanking sequence was analyzed for possible regulatory elements that would control gene expression. In Drosophila several of these elements have been shown to be involved in development and cell differentiation. The deduced amino acid sequence has low identity compared with the four alternatively spliced enzymes, adGSTI-1 to 1-4, from another An. dirus GST gene adgstAS1. The percent identities are 30-40% and 11-12% comparing adGST4-1 to insect GSTs from Delta and Sigma classes, respectively. Enzyme characterization of adGST4-1 shows it to be distinct from the other An. dirus GSTs because of low enzyme activity for customary GST substrates including 1-chloro-2, 4-dinitrobenzene (CDNB). However, this enzyme has a greater affinity of interaction with pyrethroids compared to the other An. dirus GSTs. © 2002 Elsevier Science Ltd. All rights reserved.