Browse > Article
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;
Citations & Related Records
연도 인용수 순위
  • Reference
1 B. Mannervik, Y. C. Awasthi, P. G. Board, J. D. Hayes, C. Ilio, B. Ketterer, I. Listowsky, R. Morgenstern, M. Muramatsu, W. R. Pearson, C. B. Pickett, K. Sato, M. Widersten and C. R. Wolf, Biochem. J., 282, 305-308(1992)   DOI   ScienceOn
2 R. N. Armstrong, Chem. Res. Toxicol., 10, 2-18(1997)   DOI   PUBMED   ScienceOn
3 R. Leurs, D. Donnell, H. Timmerman, A. Bast, J. Pharm. Pharmacol., 41, 388-393(1989)   DOI   PUBMED
4 G. Grove, R. P. Zarlengo, K. P. Timmerman, N. Q. Li, M. F. Tam and C. P. Tu, Nucleic Acids Res., 16, 425- 438(1988)   DOI   ScienceOn
5 G. P. Irzyk and E. P. Fuerst, Plant physiol., 102, 803- 810(1993)   DOI   ScienceOn
6 C. Y. Lee, L. Johnson, R. H. Cox, J. D. McKinney and S. M. Lee, J. Biol. Chem., 256, 8110-8116(1981)   PUBMED
7 S. H. Hong, H. J. Park and K. H. Kong, Comp. Biochem Physiol., 122, 21-27(1999)   DOI   ScienceOn
8 B. Mannervik and U. H. Danielson, CRC Crit. Rev. Biochem., 23, 283-337(1988)   DOI   PUBMED
9 R. C. Fahey and A. R. Sundquist, Adv Enzymol. Rel. Areas Mol. Biol., 64, 1-53(1991)   PUBMED   ScienceOn
10 M. Izuka, Y. Inoue, K. Murata and A. Kimura, J. Bacteriol., 171, 6039-6042(1989)   DOI   PUBMED
11 K. H. Kong, H. Inoue and K. Takahashi, Biochem. Biophys. Res. Commun., 81, 748-755(1991)
12 P. Reinemer, L. Prade, P. Hof, T. Neuefeind, R. Huber, R. Zettl, K. Palme, J. Schell, I. Koelln, H. D. Bartunik and B. Bieseler, J. Mol Biol., 255, 289-309(1991)   DOI   ScienceOn
13 H. Schramm, L. W. Robertson and F. Oesch, Biochem. Pharmacol., 34, 3735-3739(1995)   DOI   ScienceOn
14 B. Mannervik, Methods Enzymol., 113, 490-495(1985.)   DOI   PUBMED   ScienceOn
15 G. J. Beckett and J. D. Hayes, Adv. Chim. Chem., 30, 281-380(1993)
16 D. Sheehan, G. Meade, V. M. Foley and C. A. Dowd, Biochem. J., 360, 1-16(2001)   DOI   ScienceOn
17 D. E. Riechers, G. P. Irzyk, S. S. Jones and E. P. Fuerst, Plant physiol., 114, 1461-1470(1997)   DOI   ScienceOn
18 M. F. Lopez, W. F. Patton, W. B. Sawlivich, H. Erdjument-Bromage, P. Barry, K. Gmyrek, T. Hines, P. Tempst and W. M. Skea, Biochem. Biophys. Acta., 1205, 29-38(1994)   DOI   PUBMED   ScienceOn
19 K. Hahn and G. Strittmatter, Eur. J. Biochem., 226, 619- 626(1994)   DOI   ScienceOn
20 R. E. Moore, M. S. Davies, K. M. O'Connell, E. I. Harding, R. C. Wiegand and D. C. Tiemeier, Nucleic Acids Res., 14, 7227-7235(1986)   DOI   ScienceOn
21 J. M. Overbaugh, P. E. Lau, V. A. Marino and R. Fall, Arch. Biochem. Biophys., 261, 227-234(1988)   DOI   ScienceOn
22 C. Di Ilio, A. Aceto, N. Allocati, R. Piccolomini, T. Bucciarelli, B. Dragani, A. Faraone, P. Sacchetta, R. Petruzzelli and G. Federici, Arch. Biochem. Biophys., 305, 110-114(1993)   DOI   ScienceOn
23 H. Itzhaki and W. R. Woodson, Plant Mol. Biol., 22, 43-58(1993)   DOI   ScienceOn
24 T. Aoyagi, T. Aoyama, F. Kojima, N. Matsuda, M. Maruyama, M. Hamada and T. Takeuchi, J. Antibiot., 45, 1385-1390(1992)   DOI   PUBMED
25 A. Aceto, B. Dragani, T. Bucciarelli, P. Sacchetta, F. Martini, S. Angelucci, F. Amicarelli, M. Miranda and C. Di Ilio, Biochem. J., 289, 417-422(1993)   DOI   ScienceOn
26 K. H. Kong, H. Inoue and K. Takahashi, Biochem. Biophys. Res. Commun., 181, 748-755(1991)   DOI   ScienceOn
27 W. H. Habig and W. B. Jakoby, Methods Enzymol., 77, 398-405(1981)   DOI   PUBMED   ScienceOn
28 U. K. Laemmli, Nature(London), 227, 680-685(1970)   DOI   PUBMED   ScienceOn
29 F. Droog, A. Spek, A. van der Kooy, A. de Ruyter, H. Hoge, K. Libbenga, P. Hooykaas and B. van der Zaal, Plant Mol. Biol., 29, 413-429(1995)   DOI   ScienceOn
30 D. J. Meyer, B. Coles, S. E. Pemble, K. S. Gilmore, G. M. Fraser and B. Ketterer, Biochem. J., 274, 409-414(1991)   DOI   ScienceOn
31 G. Irzyk, S. Potter, E. Ward and E. P. Fuerst, Plant Physiol., 107, 311-31(1993)   DOI   ScienceOn
32 T. J. Mozer, D. C. Tiemeier and E. G. Jaworski, Biochemistry, 22, 1068-1072(1983)   DOI   ScienceOn
33 M. Nishida, K. H. Kong, H. Inoue and K. Takahashi, J. Biol. Chem., 269, 32536-32541(1994)   PUBMED
34 K. Ando, M. Honma, S. Chiba, S. Tahara and J. Mizutani, Agric. Biol. Chem., 52, 135-139(1988.)   DOI
35 D. Bartling, R. Radzio, U. Steiner and E. W. Weiler, Eur. J. Biochem., 216, 579-586(1993)   DOI   ScienceOn
36 G. L. Lamoureux and D. G. Rusness, J. Agric. Food Chem., 28, 1057-1070(1980)   DOI   PUBMED