Characterization of glutathione S-transferase of the rice leaffolder moth, Cnaphalocrocis medinalis (Lepidoptera: Pyralidae): Comparison of its properties of glutathione S-transferases from other lepidopteran insects

Kohji Yamamoto, Satoshi Teshiba, Yoichi Aso

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

An enzyme that possesses the glutathione S-transferase (GST) activity was found in the rice leaffolder moth, Cnaphalocrocis medinalis. The enzyme was purified to homogeneity for the first time by ammonium sulfate fractionation and affinity chromatography. The resultant enzyme revealed a single band with a molecular mass of 24 kDa by SDS-polyacrylamide gel electrophoresis under reduced conditions. When assayed with 1-chloro-2,4-dinitrobenzene, a universal substrate for GST, the purified GST had an optimum pH at 8.0, and was fairly stable at pH 3-10 and at temperatures below 50 °C. The enzyme was also able to conjugate glutathione to 4-hydroxynonenal, a cytotoxic lipid peroxidation product. The present GST was inhibited by fenitrothion, permethrin, and deltamethrin, suggesting that the GST could be involved in metabolizing these organophosphorus and pyrethroid insecticides.

Original languageEnglish
Pages (from-to)125-128
Number of pages4
JournalPesticide Biochemistry and Physiology
Volume92
Issue number3
DOIs
Publication statusPublished - Nov 1 2008

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Health, Toxicology and Mutagenesis

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