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

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.