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Purification and characterization of a novel sigma‐class glutathione S ‐transferase of the fall webworm, Hyphantria cunea
Author(s) -
Yamamoto K.,
Miake F.,
Aso Y.
Publication year - 2007
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.1439-0418.2007.01150.x
Subject(s) - hyphantria , biology , glutathione , biochemistry , enzyme , incubation , chromatofocusing , enzyme assay , glycine , isoelectric point , amino acid , botany , lepidoptera genitalia
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.