Purification and characterization of a novel sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea

K. Yamamoto, F. Miake, Y. Aso

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

An enzyme that possesses glutathione S-transferase (GST) activity was found in the fall webworm, Hyphantria cunea. The enzyme was purified to homogeneity for the first time by ammonium sulphate fractionation and affinity chromatography. The N-terminal sequence of the purified protein was similar to those of Sigma-class GSTs. The purified GST retained more than 75% of its original GST activity after incubation at pH 5-8. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. The enzyme was able to catalyse the reaction of glutathione with 1-chloro-2,4-dinitrobenzene, a universal substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation.

Original languageEnglish
Pages (from-to)466-471
Number of pages6
JournalJournal of Applied Entomology
Volume131
Issue number7
DOIs
Publication statusPublished - Aug 1 2007

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Hyphantria cunea
glutathione transferase
enzymes
affinity chromatography
ammonium sulfate
glutathione
fractionation
lipid peroxidation
amino acid sequences
temperature

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Insect Science

Cite this

Purification and characterization of a novel sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea. / Yamamoto, K.; Miake, F.; Aso, Y.

In: Journal of Applied Entomology, Vol. 131, No. 7, 01.08.2007, p. 466-471.

Research output: Contribution to journalArticle

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