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

Kohji Yamamoto, Sumiharu Nagaoka, Yutaka Banno, Yoichi Aso

研究成果: Contribution to journalArticle

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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.

元の言語英語
ページ(範囲)461-467
ページ数7
ジャーナルComparative Biochemistry and Physiology - C Toxicology and Pharmacology
149
発行部数4
DOI
出版物ステータス出版済み - 5 1 2009

All Science Journal Classification (ASJC) codes

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

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