- P-ISSN 1225-0163
- E-ISSN 2288-8985
- P-ISSN1225-0163
- E-ISSN2288-8985
- SCOPUS, ESCI, KCI
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Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
2009, v.22 no.3, pp.228-234
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(2009). Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase. Analytical Science and Technology, 22(3), 228-234.
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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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