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Characterization of glutathione S ‐transferase in the saturniid moth, Samia Cynthia pryeri (Lep.: Saturniidae)
Author(s) -
Yamamoto K.,
Miake F.,
Aso Y.,
Teshiba S.
Publication year - 2009
Publication title -
journal of applied entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 60
eISSN - 1439-0418
pISSN - 0931-2048
DOI - 10.1111/j.1439-0418.2008.01331.x
Subject(s) - biology , deltamethrin , enzyme , biochemistry , chromatography , fenitrothion , affinity chromatography , saturniidae , sodium dodecyl sulfate , microbiology and biotechnology , chemistry , pesticide , lepidoptera genitalia , botany , agronomy
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.