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http://dx.doi.org/10.5806/AST.2009.22.3.228

Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase  

Park, Hee-Joong (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
Lee, Hee-Jin (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
Kong, Kwang-Hoon (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
Publication Information
Analytical Science and Technology / v.22, no.3, 2009 , pp. 228-234 More about this Journal
Abstract
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.
Keywords
enzymatic characterization; glutathione S-tranferase; Brassica oleracea; purification; substrate specificity; inhibition effect;
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