Analysis on the substrate specificity and inhibition effect of Brassica oleracea glutathione S-Transferase
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
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.
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.
참고문헌 (36)
- B. Mannervik, , CRC Crit. Rev. Biochem., 23, pp.283~337 (1988)
- R. C. Fahey, , Adv Enzymol. Rel. Areas Mol. Biol., 64, pp.1~53 (1991)
- B. Mannervik, , Biochem. J, (282), pp.305~308 (1992)
- G. J. Beckett, , Adv. Chim. Chem., 30, pp.281~380 (1993)
- R. N. Armstrong, , Chem. Res. Toxicol., 10, pp.2~18 (1997)
- G. L. Lamoureux, , J. Agric. Food Chem., 28, pp.1057~1070 (1980)
- R. Leurs, , J. Pharm. Pharmacol., 41, pp.388~393 (1989)
- T. J. Mozer, , Biochemistry, (22), pp.1068~1072 (1983)
- R. E. Moore, , Nucleic Acids Res., 14, pp.7227~7235 (1986)
- G. Grove, , Nucleic Acids Res., 16, pp.425~438 (1988)
- M. Izuka, , J. Bacteriol., 171, pp.6039~6042 (1989)
- G. P. Irzyk, , Plant physiol., 102, pp.803~810 (1993)
- G. Irzyk, , Plant Physiol., 107, pp.311~331 (1993)
- D. Sheehan, , Biochem. J., 360, pp.1~16 (2001)
- D. E. Riechers, , Plant physiol., 114, pp.1461~1470 (1997)
- F. Droog, , Plant Mol. Biol., 29, pp.413~429 (1995)
- H. Itzhaki, , Plant Mol. Biol., 22, pp.43~58 (1993)
- M. F. Lopez, , Biochem. Biophys. Acta, 1205, pp.29~38 (1994)
- H. Schramm, , Biochem. Pharmacol., 34, pp.3735~3739 (1995)
- T. Aoyagi, , J. Antibiot, 45, pp.1385~1390 (1992)
- W. H. Habig, , Methods Enzymol., 77, pp.398~405 (1981)
- B. Mannervik, , Methods Enzymol., 113, pp.490~495 (1985)
- S. H. Hong, , Comp. Biochem Physiol., 122, pp.21~27 (1999)
- U. K. Laemmli, , Nature, (227), pp.680~685 (1970)
- K. H. Kong, , Biochem. Biophys. Res. Commun., 181, pp.748~755 (1991)
- M. Nishida, , J. Biol. Chem., 269, pp.32536~32541 (1994)
- J. M. Overbaugh, , Arch. Biochem. Biophys., 261, pp.227~234 (1988)
- C. Di Ilio, , Arch. Biochem. Biophys., 305, pp.110~114 (1993)
- K. Ando, , Agric. Biol. Chem., 52, pp.135~139 (1988)
- C. Y. Lee, , J. Biol. Chem., 256, pp.8110~8116 (1981)
- A. Aceto, , Biochem. J., 289, pp.417~422 (1993)
- D. Bartling, , Eur. J. Biochem., 216, pp.579~586 (1993)
- K. Hahn, , Eur. J. Biochem., 226, pp.619~626 (1994)
- K. H. Kong, , Biochem. Biophys. Res. Commun., 81, pp.748~755 (1991)
- P. Reinemer, , J. Mol Biol., 255, pp.289~309 (1991)
- D. J. Meyer, , Biochem. J, 274, pp.409~414 (1991)