생명과학회지 (Journal of Life Science)

  • 제12권3호
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  • Pages.281-287
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  • 2002
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  • 1225-9918(pISSN)
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  • 2287-3406(eISSN)
한국생명과학회 (Korean Society of Life Science)
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포유동물 1,4-벤조퀴논 환원효소에 의한 아릴니트로소 화합물의 생변환

Biotransformation of Arylnitroso Compound by Mammalian 1,4-Benzoquinone Reductase

  • 발행 : 2002.06.01
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초록

소 간으로부터 퀴논 환원효소를 정제하였으며 정제된 효소는 벤조퀴논과 나프토퀴논 뿐만 아니라 페난트렌 퀴논의 환원도 촉매하였다. 소 간으로부터 정제된 퀴논 환원 효소는 아릴니트로소 화합물의 생변환을 촉매하였으며 반응 생성물은 TLC, GC, GC-MS, NMR을 사용하여 확인되었다. 이 반응은 포유동물 퀴논 환원효소의 강력한 저해제인 Cibacron blue 3GA나 dicumarol에 의하여 크게 저해되었다.

Quinone reductase was purified to homogeneity from bovine liver and the purified enzyme catalyzed the reduction of phenanthrenequinone as well as benzo- and naphthoquinones. The enzyme catalyzed the biotransformation of arylnitroso nitroso compound and the reaction product was identified by TLC, GC, CC-MS and NMR. The reaction was almost entirely inhibitable by Cibacron blue 3GA or dicumarol, potent inhibitors of mammalian quinone reductase.

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참고문헌

  1. Tetrahedron Lett v.36 Selective reduction of aromatic nitroso compounds with baker's yeast under neutral condiction. Baik, W., J. Rhee, S. Lee, N. Lee, B. Kim;K. Kim https://doi.org/10.1016/0040-4039(95)00398-V
  2. J. Biol. Chem v.264 Rat liver NAD(P)H: quinone reductase Bayney, R.M., M.R. Motron, L.V. Favreau;C. B. Pickett
  3. Anal. Biochem v.72 A rapid and sensitive method for quantitation of microgram quantities of protein utlilizing the principle of protein-dye binding. Bradford, M. M https://doi.org/10.1016/0003-2697(76)90527-3
  4. Arch. Biochem. Biophys v.331 1,4-Benzoquinone reductase from the basidiomycete Phanerochate chrysosporium : Spectral and kinetic analysis Brock, B.J;M.H. Gold https://doi.org/10.1006/abbi.1996.0279
  5. Appl. Environ. Microbiol v.61 Purification and characterization of a 1,4-benzoquinone reductase from the basidiomycete Phanerochate chrysosporium Brock, B.J., S. Reible;M.H. Gold
  6. Toxi. Appl. Pharm v.124 Role of quinone reductase in in vivo ethanol metabolism and toxicity Chung, J.H., Y.N. Cha;R.J. Rubin https://doi.org/10.1006/taap.1994.1015
  7. J. Gen. Microbiol v.137 Purification and partial characterization of an intracellular NADH : quinone oxidoreductase from Phanerochaete chrysosporium Constam, D., A. Muheim, W. Zimmermann;A. Fiechter https://doi.org/10.1099/00221287-137-9-2209
  8. Carcinogenesis v.7 1,2-Dithiol-3-thione analogs: effects on NAD(P)H : quinone reductase and glutathione levels in murine hepatoma cells De Long, M. J., P. Dolan, A. B. Santamaria;E. Bueding https://doi.org/10.1093/carcin/7.6.977
  9. J. Biol. Chem v.270 The rat quinone reductase antioxidant response element Favreau, L.V;C.B. Pickett https://doi.org/10.1074/jbc.270.41.24468
  10. Carcinogenesis v.12 Induction of NAD(P)H : quinone reductase in human peripheral blood lymphocytes Gordon, G.B., H.J. Prochaska;L. Y.-S. Yang https://doi.org/10.1093/carcin/12.12.2393
  11. Arch. Biochem. Biophys v.207 Biospecific adsorption of hepatic DT-diaphorase on immobilized dicoumarol Hojeberg, B., K. Blomberg, S. Stenberg;C. Lind https://doi.org/10.1016/0003-9861(81)90026-6
  12. J. Biochem. Mol. Biol v.32 Reduction of Nitrosoarene by purified NAD(P)H-quinone oxidoreductase Kim, K;H. Suk
  13. J. Biochem. Mol. Biol v.33 Reduction of azobenzene by purified bovine liver quinone reductase Kim, K;H.-Y. Shin
  14. Biol. Pharm. Bull v.22 DT-diaphorase-like quinone reductase in rat plasma Kitamura, S., A. Terada, H. Kamio, K. Sugihara, N. Koga;S. Ohta
  15. Nature v.227 Cleavage of structural proteins during the awwembly of the head of bacteriophage T4 Laemmli, U. K https://doi.org/10.1038/227680a0
  16. Toxi. Appl. Pharm v.122 Menadione toxicity in two mouse liver established cell lines having striking genetic differences in quinone reductase activity and glutathione concentrations Liu, R. -M., D. W. Nebert;H. G. Shertzer https://doi.org/10.1006/taap.1993.1177
  17. Biochemistry v.31 Inhibition of NAD(P)H : (quinone-acceptor) oxidore-ductase by Cibacron blue and related anthraquinone dyes: a structure-activity study Prestera, T., H. J. Prochaska;P. Talalay https://doi.org/10.1021/bi00118a027
  18. Proc. Natl. Acad. Sci v.90 Chemical and molecular regulation of enzymes that detoxify carcinogens Presters, T., W. D. Holtzclaw, Y. Zhang;P. Talalay https://doi.org/10.1073/pnas.90.7.2965
  19. J. Biol. Chem v.261 Purification and characterization of two isofunctional forms of NAD(P)H: quinone reductase from mouse liver Prochaska, H.J;P. Talalay
  20. Fd. Chem. Toxic v.32 Effect of metanil yellow, orange II and their blend on hepatic xenobiotic metabolizing enzymes in rats Ramchandani, S., M. Das;S. K. Khanna https://doi.org/10.1016/0278-6915(94)90114-7
  21. Eur. J. Biochem v.195 The human dioxin-inducible NAD(P)H: quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4 Shaw, P. M., A. Reiss, M. Adesnik, D. W. Nebert, J. Schembri;A. K. Jaiseal https://doi.org/10.1111/j.1432-1033.1991.tb15691.x
  22. Eur. J. Biochem v.234 Purification and properties of NAD(P)H: quinone-acceptor oxidoreductase of sugarbeet cells Trost, P., Bonora, S. Scagliarini;P. Pupillo https://doi.org/10.1111/j.1432-1033.1995.452_b.x
  23. Appl. Environ. Micro v.58 Degradation of 2,4-dinitrotoluene by the lignindegrading fungus phanerochaete chrysosporium Valli, K., B. J. Brock, D. K. Joshi;M. H. Gold
  24. J. Bacterio v.174 Degradation of 2,7-dichlorodibenzo-Ρ-dioxin by the lignindegrading basidiomycete Phanerochaete chrysosporium Valli, K., H. Wariishi;M. H. Gold
  25. J. Bacterio v.173 Degradation of 2,4-dichlorophenol by the lignin-degrading fungus Phanerochaete chrysosporium. Valli, K;M. H. Gold
  26. Proc. Natl. Acad. Sci v.89 A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure Zhang, Y., P. Talalay, C. -G. Cho;G. H. Posner https://doi.org/10.1073/pnas.89.6.2399