Characterization of glutathione S-transferase in the saturniid moth, Samia Cynthia pryeri (Lep. Saturniidae)

K. Yamamoto, F. Miake, Y. Aso, S. Teshiba

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

An enzyme, which possesses glutathione S-transferase (GST) activity, has been found in the midgut of the saturniid moth, Samia cynthia pryeri. The enzyme was initially purified into homogeneity by ammonium sulphate fractionation, affinity chromatography, and ion-exchange chromatography. The resulting enzyme revealed a single band with a molecular mass of 23 kDa by sodium dodecyl sulfate polyacrylamide electrophoresis under reduced conditions. When tested with 1-chloro-2,4-dinitrobenzene, a universal substrate of GST, the purified remnants had an optimum pH of 8.0 for enzymatic activity, and was fairly stable at pH 5-9 and at temperatures below 40°C. The enzyme was also responsive to 4-hydroxynonenal, a cytotoxic lipid-peroxidation product. The present GST was inhibited by organophosphorus and pyrethroid insecticides including fenitrothion, permethrin and deltamethrin.

Original languageEnglish
Pages (from-to)278-283
Number of pages6
JournalJournal of Applied Entomology
Volume133
Issue number4
DOIs
Publication statusPublished - May 1 2009

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Insect Science

Fingerprint Dive into the research topics of 'Characterization of glutathione S-transferase in the saturniid moth, Samia Cynthia pryeri (Lep. Saturniidae)'. Together they form a unique fingerprint.

  • Cite this