Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori

Kohji Yamamoto, Sumiharu Nagaoka, Yutaka Banno, Yoichi Aso

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

A cDNA encoding an omega-class glutathione S-transferase of the silkmoth, Bombyx mori (bmGSTO), was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and deduced for amino acid sequence, which revealed 40, 40, and 39% identities to omega-class GSTs from human, pig, and mouse, respectively. A recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rbmGSTO was able to catalyze the biotranslation of glutathione with 1-chloro-2,4-dinitrobenzene, a model substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation. This enzyme was shown to have high affinity for organophosphorus insecticide and was present abundantly in silkmoth strain exhibiting fenitrothion resistance. These results indicate that bmGSTO could be involved in the increase in level of insecticide resistance for lepidopteran insects.

Original languageEnglish
Pages (from-to)461-467
Number of pages7
JournalComparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume149
Issue number4
DOIs
Publication statusPublished - May 1 2009

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Toxicology
  • Cell Biology
  • Health, Toxicology and Mutagenesis

Fingerprint Dive into the research topics of 'Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori'. Together they form a unique fingerprint.

  • Cite this