Expression and Characterization of a Sigma-Class Glutathione S-Transferase of the Fall Webworm, Hyphantria cunea
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概要
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A cDNA encoding glutathione S-transferase (GST) of the fall webworm, Hyphantria cunea, was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone (hcGST) was sequenced and deduced for amino acid sequence, which revealed 87, 59, and 42% identities to Sigma-class GSTs from Bombyx mori, Manduca sexta, and Blattella germanica respectively. A recombinant hcGST protein (rhcGST) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rhcGST retained more than 75% of its original GST activity after incubation at pHs 6 to 11. Incubation for 30 min at temperatures below 50 °C scarcely affected the activity. rhcGST was able to catalyze 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. We also found that as compared to B. mori Sigma-class GST, rhcGST had a higher affinity for fenitrothion, an organophosphorus insecticide.
- 社団法人 日本農芸化学会の論文
著者
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BANNO Yutaka
Institute of Genetic Resources, Kyushu University
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FUJII Hiroshi
Institute of Genetic Resources, Kyushu University
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Yamamoto K
Laboratory Of Insect Genetic Resources Faculty Of Agriculture Kyushu University
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Yamamoto Kohji
Institute Of Genetic Resources Graduate School Of Bioresources And Bioenvironmental Science Kyushu U
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ASO Yoichi
Faculty of Agriculture, Kyushu University Graduate School
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KOGA Katsumi
Faculty of Agriculture, Kyushu University Graduate School
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Fujimoto Hirofumi
Division Of Radiological Protection And Biology National Institute Of Infectious Diseases
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