TY - JOUR
T1 - Purification and characterization of a novel sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea
AU - Yamamoto, K.
AU - Miake, F.
AU - Aso, Y.
PY - 2007/8
Y1 - 2007/8
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34447638390&partnerID=8YFLogxK
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U2 - 10.1111/j.1439-0418.2007.01150.x
DO - 10.1111/j.1439-0418.2007.01150.x
M3 - Article
AN - SCOPUS:34447638390
SN - 0931-2048
VL - 131
SP - 466
EP - 471
JO - Journal of Applied Entomology
JF - Journal of Applied Entomology
IS - 7
ER -