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

공광훈; 박희중; 이희진

오늘 하루 그만보기

P-ISSN1225-0163
E-ISSN2288-8985
SCOPUS, ESCI, KCI

Home

Browse Articles

Article Detail

Home > Article Detail

P-ISSN 1225-0163
E-ISSN 2288-8985

e-Submission

Vol.22, No.3

PubReader PDF Citation

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

& (2009). Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase. , 22(3), 228-234.

copy

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.