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KMID : 0385520090220030228
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Analytical Science & Technology
2009 Volume.22 No. 3 p.228 ~ p.234
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Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase
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Park Hee-Joong
Lee Hee-Jin
Kong Kwang-Hoon
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Abstract
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To gain further insight into herbicide detoxification of plant, we purified a glutathione S-transferase from Brassica oleracea (BoGST) and studied its substrate specificity towards several xenobiotic compounds. The BoGST was purified to electrophoretic homogeneity with approximately 10% activity yield by DEAE-Sephacel and GSHSepharose column chromatography. The molecular weight of the BoGST was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the BoGST was significantly inhibited by S-hexyl-GSH and S-(2,4-dinitrophenyl)GSH. The substrate specificity of the BoGST displayed high activities towards CDNB, a general GST substrate and ethacrynic acid. It also exhibited GSH peroxidase activity toward cumene hydroperoxide.
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KEYWORD
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enzymatic characterization, glutathione S-tranferase, Brassica oleracea, purification, substrate specificity, inhibition effect
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