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

Fingerprint

Samia cynthia
Saturniidae
glutathione transferase
moths
enzymes
fenitrothion
pyrethroid insecticides
organophosphorus insecticides
deltamethrin
permethrin
sodium dodecyl sulfate
ion exchange chromatography
polyacrylamide
affinity chromatography
ammonium sulfate
midgut
electrophoresis
fractionation
lipid peroxidation
molecular weight

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Insect Science

Cite this

Characterization of glutathione S-transferase in the saturniid moth, Samia Cynthia pryeri (Lep. Saturniidae). / Yamamoto, K.; Miake, F.; Aso, Y.; Teshiba, S.

In: Journal of Applied Entomology, Vol. 133, No. 4, 01.05.2009, p. 278-283.

Research output: Contribution to journalArticle

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