메뉴 건너뛰기




Volumn 69, Issue 3, 2004, Pages 259-270

Effects of β-naphthoflavone, phenobarbital and dichlobenil on the drug-metabolizing system of liver and nasal mucosa of Italian water frogs

Author keywords

CYP induction and inhibition; Cytochrome P450 (CYP); Nasal mucosa phase I and II enzymes; Water frogs

Indexed keywords

ANTIBODY; BETA NAPHTHOFLAVONE; BIOLOGICAL MARKER; COUMARIN 7 HYDROXYLASE; CYTOCHROME P450; CYTOCHROME P450 1A; CYTOCHROME P450 1A1; CYTOCHROME P450 2A; DICHLOBENIL; DRUG METABOLIZING ENZYME; ETHOXYRESORUFIN DEETHYLASE; LIVER ENZYME; METHOXYRESORUFIN O DEMETHYLASE; METYRAPONE; PHENOBARBITAL; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; XENOBIOTIC AGENT;

EID: 3242792598     PISSN: 0166445X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.aquatox.2004.06.001     Document Type: Article
Times cited : (9)

References (58)
  • 2
    • 0018170362 scopus 로고
    • A single sensitive assay of ethoxycoumarin deethylation
    • Aitio A. A single sensitive assay of ethoxycoumarin deethylation. Anal. Biochem. 85:1978;488-491
    • (1978) Anal. Biochem. , vol.85 , pp. 488-491
    • Aitio, A.1
  • 3
    • 0022270572 scopus 로고
    • Differential induction cytochrome P450-dependent monooxygenase, epoxide hydrolase, glutathione transferase and UDP glucuronyl transferase activities in the liver of the rainbow trout by β-naphthoflavone or clophen A50
    • Andersson T., Pesonen M., Johansson C. Differential induction cytochrome P450-dependent monooxygenase, epoxide hydrolase, glutathione transferase and UDP glucuronyl transferase activities in the liver of the rainbow trout by β-naphthoflavone or clophen A50. Biochem. Pharmacol. 34:1985;3309-3314
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3309-3314
    • Andersson, T.1    Pesonen, M.2    Johansson, C.3
  • 5
    • 0028227327 scopus 로고
    • Two unique CYP 1 genes are expressed in response to 3-methyl-cholantrene treatment in rainbow trout
    • Berndtson A.K., Chen T.T. Two unique CYP 1 genes are expressed in response to 3-methyl-cholantrene treatment in rainbow trout. Arch. Biochem. Biophys. 310:1994;187-195
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 187-195
    • Berndtson, A.K.1    Chen, T.T.2
  • 6
    • 0025212185 scopus 로고
    • Irreversible binding and toxicity of the herbicide dichlobenil (2,6-dichlorobenzonitrile) in the olfactory mucosa of mice
    • Brandt I., Brittebo E.B., Feil V.J., Bakke J.E. Irreversible binding and toxicity of the herbicide dichlobenil (2,6-dichlorobenzonitrile) in the olfactory mucosa of mice. Toxicol. Appl. Pharmacol. 103:1990;491-501
    • (1990) Toxicol. Appl. Pharmacol. , vol.103 , pp. 491-501
    • Brandt, I.1    Brittebo, E.B.2    Feil, V.J.3    Bakke, J.E.4
  • 7
    • 0031770433 scopus 로고    scopus 로고
    • Rainbow trout cytochrome P450s: Purification, molecular aspects, metabolic activity, induction and role in environmental monitoring
    • Buhler D.R., Buhler J.L. Rainbow trout cytochrome P450s: purification, molecular aspects, metabolic activity, induction and role in environmental monitoring. Comp. Biochem. Physiol. 121C:1998;107-137
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 107-137
    • Buhler, D.R.1    Buhler, J.L.2
  • 8
    • 0026622869 scopus 로고
    • Multiplicity of UDP-glucuronosyltransferases in fish
    • Clarke D.J., George S.G., Burchell B. Multiplicity of UDP-glucuronosyltransferases in fish. Biochem. J. 284:1992;417-423
    • (1992) Biochem. J. , vol.284 , pp. 417-423
    • Clarke, D.J.1    George, S.G.2    Burchell, B.3
  • 9
    • 0020620013 scopus 로고
    • UDP-glucuronosyltransferase activity and bilirubin conjugation in the bullfrog
    • Cole K.D., Little G.H. UDP-glucuronosyltransferase activity and bilirubin conjugation in the bullfrog. Biochem. J. 212:1983;265-269
    • (1983) Biochem. J. , vol.212 , pp. 265-269
    • Cole, K.D.1    Little, G.H.2
  • 10
    • 0029153416 scopus 로고
    • Physiological and histological recovery of the olfactory mucosa of the frog after a dichlobenil injection
    • Delaleu J.C., Sicard G. Physiological and histological recovery of the olfactory mucosa of the frog after a dichlobenil injection. Chem. Senses. 20:1995;433-440
    • (1995) Chem. Senses , vol.20 , pp. 433-440
    • Delaleu, J.C.1    Sicard, G.2
  • 11
    • 0029982314 scopus 로고    scopus 로고
    • Metabolic activation of 2,6-dichlorobenzonitrile, an olfactory-specific toxicant, by rat, rabbit, and human cytochromes
    • Ding X., Spink D.C., Bhama J.K., Sheng J.J., Vaz A.D.N., Coon M.J. Metabolic activation of 2,6-dichlorobenzonitrile, an olfactory-specific toxicant, by rat, rabbit, and human cytochromes. Mol. Pharmacol. 49:1996;1113-1121
    • (1996) Mol. Pharmacol. , vol.49 , pp. 1113-1121
    • Ding, X.1    Spink, D.C.2    Bhama, J.K.3    Sheng, J.J.4    Vaz, A.D.N.5    Coon, M.J.6
  • 12
    • 0025775790 scopus 로고
    • Metabolic activation of the herbicide dichlobenil in the olfactory mucosa of mice and rats
    • Eriksson C., Brittebo E.B. Metabolic activation of the herbicide dichlobenil in the olfactory mucosa of mice and rats. Chem. Biol. Interact. 79:1991;165-177
    • (1991) Chem. Biol. Interact. , vol.79 , pp. 165-177
    • Eriksson, C.1    Brittebo, E.B.2
  • 13
    • 0031737337 scopus 로고    scopus 로고
    • The microsomal mixed function oxidase system of amphibians and reptiles: Components, activities and induction
    • Ertl R.P., Winston G.W. The microsomal mixed function oxidase system of amphibians and reptiles: components, activities and induction. Comp. Biochem. Physiol. 121C:1998;85-105
    • (1998) Comp. Biochem. Physiol. , vol.121 , pp. 85-105
    • Ertl, R.P.1    Winston, G.W.2
  • 14
    • 0033230925 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of cDNAs coding for 3-methylcholantrene-inducible cytochromes P450 in Xenopus laevis liver
    • Fujita Y., Ohi H., Murayama N., Saguchi K.I., Higuchi S. Molecular cloning and sequence analysis of cDNAs coding for 3-methylcholantrene-inducible cytochromes P450 in Xenopus laevis liver. Arch. Biochem. Biophys. 371:1999;24-28
    • (1999) Arch. Biochem. Biophys. , vol.371 , pp. 24-28
    • Fujita, Y.1    Ohi, H.2    Murayama, N.3    Saguchi, K.I.4    Higuchi, S.5
  • 15
    • 0000818292 scopus 로고
    • Cytochrome P450 in rodents
    • Schenkman, B., Greim, H. (Eds.), Springer Verlag, Berlin
    • Funae, Y., Imaoka, S., 1993. Cytochrome P450 in rodents. In: Schenkman, B., Greim, H. (Eds.), Handbook of Experimental Pharmacology, vol. 105. Springer Verlag, Berlin, pp. 221-223.
    • (1993) Handbook of Experimental Pharmacology , vol.105 , pp. 221-223
    • Funae, Y.1    Imaoka, S.2
  • 16
    • 0024417435 scopus 로고
    • Comparative aspects of the mammalian cytochrome P450 IV gene family
    • Gibson G.G. Comparative aspects of the mammalian cytochrome P450 IV gene family. Xenobiotica. 19:1989;1123-1148
    • (1989) Xenobiotica , vol.19 , pp. 1123-1148
    • Gibson, G.G.1
  • 17
    • 0034665826 scopus 로고    scopus 로고
    • Cytochrome P450-dependent monooxygenase activities and their inducibility by classic P450 inducers in the liver, kidney, and nasal mucosa of male adult ring-necked pheasants
    • Giorgi M., Marini S., Longo V., Mazzaccaro A., Amato G., Gervasi P.G. Cytochrome P450-dependent monooxygenase activities and their inducibility by classic P450 inducers in the liver, kidney, and nasal mucosa of male adult ring-necked pheasants. Toxicol. Appl. Pharmacol. 167:2000;237-245
    • (2000) Toxicol. Appl. Pharmacol. , vol.167 , pp. 237-245
    • Giorgi, M.1    Marini, S.2    Longo, V.3    Mazzaccaro, A.4    Amato, G.5    Gervasi, P.G.6
  • 18
    • 0025067462 scopus 로고
    • Molecular genetics of the P450 superfamily
    • Gonzales F.J. Molecular genetics of the P450 superfamily. Pharmacol. Ther. 45:1989;1-38
    • (1989) Pharmacol. Ther. , vol.45 , pp. 1-38
    • Gonzales, F.J.1
  • 19
    • 0001144384 scopus 로고
    • Evolutionary genetics of the Rana esculenta complex
    • Dawley, R.M., Bogart, J.P. (Eds.), New York State Museum, Albany, NY
    • Graf, J.D., Polls Pelaz, M., 1989. Evolutionary genetics of the Rana esculenta complex. In: Dawley, R.M., Bogart, J.P. (Eds.), Evolution and Ecology of Unisexual Vertebrates. New York State Museum, Albany, NY, pp. 289-302.
    • (1989) Evolution and Ecology of Unisexual Vertebrates , pp. 289-302
    • Graf, J.D.1    Polls Pelaz, M.2
  • 20
    • 0031862390 scopus 로고    scopus 로고
    • Purification and characterization of heterologously expressed mouse CYP2A5 and CYP2G1: Role in metabolic activation of acetaminophen and 2,6-diclhlorobenzonitrile in mouse olfactory mucosal microsomes
    • Gu J., Zhang Q.Y., Genter M.B., Lipinskas T.W., Negishi M., Nebert D.W., Ding X. Purification and characterization of heterologously expressed mouse CYP2A5 and CYP2G1: role in metabolic activation of acetaminophen and 2,6-diclhlorobenzonitrile in mouse olfactory mucosal microsomes. J. Pharmacol. Exp. Ther. 285:1998;1287-1295
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 1287-1295
    • Gu, J.1    Zhang, Q.Y.2    Genter, M.B.3    Lipinskas, T.W.4    Negishi, M.5    Nebert, D.W.6    Ding, X.7
  • 21
    • 0016268812 scopus 로고
    • Glutathione transferase, the first step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. Glutathione transferase, the first step in mercapturic acid formation. J. Biol. Chem. 249:1974;7140-7149
    • (1974) J. Biol. Chem. , vol.249 , pp. 7140-7149
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 23
    • 0021253492 scopus 로고
    • An alternative 7-ethoxyresorufin O-deethylase activity assay: A continuous visible spectrophotometric method for measurement of cytochrome P450 monooxygenase activity
    • Klotz A.V., Stegeman J.J., Walsh C. An alternative 7-ethoxyresorufin O-deethylase activity assay: a continuous visible spectrophotometric method for measurement of cytochrome P450 monooxygenase activity. Anal. Biochem. 140:1984;138-145
    • (1984) Anal. Biochem. , vol.140 , pp. 138-145
    • Klotz, A.V.1    Stegeman, J.J.2    Walsh, C.3
  • 24
    • 0023216022 scopus 로고
    • Monoclonal antibodies to ethanol-induced rat liver cytochrome P450 that metabolize aniline and nitrosamines
    • Ko I.Y., Park S.S., Song B.J., Patten C., Tan Y., Han Y.C., Yang C.S., Gelboin H.V. Monoclonal antibodies to ethanol-induced rat liver cytochrome P450 that metabolize aniline and nitrosamines. Cancer Res. 47:1987;3101-3109
    • (1987) Cancer Res. , vol.47 , pp. 3101-3109
    • Ko, I.Y.1    Park, S.S.2    Song, B.J.3    Patten, C.4    Tan, Y.5    Han, Y.C.6    Yang, C.S.7    Gelboin, H.V.8
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0017148506 scopus 로고
    • Purification and immunochemical characterization of aldehyde dehydrogenase from 2-acetylaminofluorene-induced rat hepatomas
    • Lindahl R., Feinstein A. Purification and immunochemical characterization of aldehyde dehydrogenase from 2-acetylaminofluorene-induced rat hepatomas. Biochem. Biophys. Acta. 452:1976;345-355
    • (1976) Biochem. Biophys. Acta , vol.452 , pp. 345-355
    • Lindahl, R.1    Feinstein, A.2
  • 27
    • 0029862553 scopus 로고    scopus 로고
    • Baculovirus-mediated expression and characterization of rat CYP2A3 and human CYP2A6: Role in metabolic activation of nasal toxicants
    • Liu C., Zhuo X., Gonzalez F.J., Ding X. Baculovirus-mediated expression and characterization of rat CYP2A3 and human CYP2A6: role in metabolic activation of nasal toxicants. Mol. Pharmacol. 50:1996;781-788
    • (1996) Mol. Pharmacol. , vol.50 , pp. 781-788
    • Liu, C.1    Zhuo, X.2    Gonzalez, F.J.3    Ding, X.4
  • 28
    • 0026176952 scopus 로고
    • Drug metabolizing enzymes in liver olfactory and respiratory epithelium of cattle
    • Longo V., Mazzaccaro A., Naldi F., Gervasi P.G. Drug metabolizing enzymes in liver olfactory and respiratory epithelium of cattle. J. Biochem. Toxicol. 6:1991;123-128
    • (1991) J. Biochem. Toxicol. , vol.6 , pp. 123-128
    • Longo, V.1    Mazzaccaro, A.2    Naldi, F.3    Gervasi, P.G.4
  • 29
    • 0030907692 scopus 로고    scopus 로고
    • Purification and characterization of three constitutive cytochrome P-450 isoforms from bovine olfactory epithelium
    • Longo V., Amato G., Santucci A., Gervasi P.G. Purification and characterization of three constitutive cytochrome P-450 isoforms from bovine olfactory epithelium. Biochem. J. 323:1997;65-70
    • (1997) Biochem. J. , vol.323 , pp. 65-70
    • Longo, V.1    Amato, G.2    Santucci, A.3    Gervasi, P.G.4
  • 30
    • 0022350885 scopus 로고
    • Dealkylation of pentoxyresorufin: A rapid and sensitive assay for measuring induction of cytochrome(s) P-450 by phenobarbital and other xenobiotics in the rat
    • Lubet R.A., Mayer R.T., Cameron J.W., Nims R.W., Burke M.D., Wolf T., Guengerich F.P. Dealkylation of pentoxyresorufin: a rapid and sensitive assay for measuring induction of cytochrome(s) P-450 by phenobarbital and other xenobiotics in the rat. Arch. Biochem. Biophys. 238:1985;43-48
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 43-48
    • Lubet, R.A.1    Mayer, R.T.2    Cameron, J.W.3    Nims, R.W.4    Burke, M.D.5    Wolf, T.6    Guengerich, F.P.7
  • 31
    • 0019275249 scopus 로고
    • A sensitive kinetic assay for UDP glucuronosyl transferase using 1-naphthol as substrate
    • Mackenzie P.I., Hanninen O. A sensitive kinetic assay for UDP glucuronosyl transferase using 1-naphthol as substrate. Anal. Biochem. 109:1980;362-368
    • (1980) Anal. Biochem. , vol.109 , pp. 362-368
    • MacKenzie, P.I.1    Hanninen, O.2
  • 32
    • 0030936838 scopus 로고    scopus 로고
    • Effects of dichlobenil on ultrastructural morphology and cell replication in the mouse olfactory mucosa
    • Mancuso M., Giovanetti A., Brittebo E.B. Effects of dichlobenil on ultrastructural morphology and cell replication in the mouse olfactory mucosa. Toxicol. Pathol. 25:1997;186-194
    • (1997) Toxicol. Pathol. , vol.25 , pp. 186-194
    • Mancuso, M.1    Giovanetti, A.2    Brittebo, E.B.3
  • 33
    • 77957003927 scopus 로고
    • 5 reductase from pig liver
    • Estabrook, R.W., Pulman, E.E. (Eds.), Academic Press, New York
    • 5 reductase from pig liver. In: Estabrook, R.W., Pulman, E.E. (Eds.), Methods in Enzymology, vol. 10. Academic Press, New York, pp. 565-573.
    • (1967) Methods in Enzymology , vol.10 , pp. 565-573
    • Masters, B.S.S.1    William, C.H.2    Kamin, H.3
  • 34
    • 0028048628 scopus 로고
    • Microsomal metabolism of N,N-diethylacetamide and N,N-dimethylacetamide and their effects on drug-metabolizing enzymes of rat liver
    • Menicagli S., Longo V., Mazzaccaro A., Gervasi P.G. Microsomal metabolism of N,N-diethylacetamide and N,N-dimethylacetamide and their effects on drug-metabolizing enzymes of rat liver. Biochem. Pharmacol. 48:1994;717-726
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 717-726
    • Menicagli, S.1    Longo, V.2    Mazzaccaro, A.3    Gervasi, P.G.4
  • 35
    • 0021872437 scopus 로고
    • Seasonal change and sex difference in laurate hydroxylase activity in frog liver microsomes
    • Miura Y. Seasonal change and sex difference in laurate hydroxylase activity in frog liver microsomes. Comp. Biochem. Physiol. 82C:1985;63-67
    • (1985) Comp. Biochem. Physiol. , vol.82 , pp. 63-67
    • Miura, Y.1
  • 36
    • 0025133548 scopus 로고
    • Cellular responses to oxidative stress: The [Ah] gene battery as a paradigm
    • Nebert D.W., Peterson D.D., Fornace A.J. Cellular responses to oxidative stress: the [Ah] gene battery as a paradigm. Environ. Health Perspect. 88:1990;13-25
    • (1990) Environ. Health Perspect. , vol.88 , pp. 13-25
    • Nebert, D.W.1    Peterson, D.D.2    Fornace, A.J.3
  • 37
    • 0037223831 scopus 로고    scopus 로고
    • Comparison of P450s from human and fugu: 420 million years of vertebrate P450 evolution
    • Nelson D.R. Comparison of P450s from human and fugu: 420 million years of vertebrate P450 evolution. Arch. Biochem. Biophys. 409:2003;18-24
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 18-24
    • Nelson, D.R.1
  • 39
    • 0021291203 scopus 로고
    • Microsomal monooxygenase system in frog livers
    • Noshiro M., Omura T. Microsomal monooxygenase system in frog livers. Comp. Biochem. Physiol. 77B:1984;761-767
    • (1984) Comp. Biochem. Physiol. , vol.77 , pp. 761-767
    • Noshiro, M.1    Omura, T.2
  • 40
    • 0002743878 scopus 로고    scopus 로고
    • Biotransformation enzymes and their induction by β-naphthoflavone in adult sea bass (Dicentrarchus labrax)
    • Novi S., Pretti C., Cognetti A.M., Longo V., Marchetti S., Gervasi P.G. Biotransformation enzymes and their induction by β-naphthoflavone in adult sea bass (Dicentrarchus labrax). Aquat. Toxicol. 41:1998;63-81
    • (1998) Aquat. Toxicol. , vol.41 , pp. 63-81
    • Novi, S.1    Pretti, C.2    Cognetti, A.M.3    Longo, V.4    Marchetti, S.5    Gervasi, P.G.6
  • 41
    • 78651165715 scopus 로고
    • The carbon-monoxide binding protein of liver microsomes. I. Evidences for its hemoprotein nature
    • Omura T., Sato R. The carbon-monoxide binding protein of liver microsomes. I. Evidences for its hemoprotein nature. J. Biol. Chem. 293:1964;2370-2378
    • (1964) J. Biol. Chem. , vol.293 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 43
    • 4243490292 scopus 로고    scopus 로고
    • Corneal and stomach expression of aldehyde dehydrogenases. from fish to mammals
    • 130132
    • Pappa A., Sophos N.A., Vasiliou V. Corneal and stomach expression of aldehyde dehydrogenases. from fish to mammals. Chem. Biol. Interact. 130132:2001;181-191
    • (2001) Chem. Biol. Interact. , pp. 181-191
    • Pappa, A.1    Sophos, N.A.2    Vasiliou, V.3
  • 44
    • 0024625072 scopus 로고
    • Genetically engineered V79 Chinese hamster cell expression of purified cytochrome P450IIB1 monooxygenase activity
    • Platt K.L., Molitor E., Dohemer J., Dogra S., Oesch F. Genetically engineered V79 Chinese hamster cell expression of purified cytochrome P450IIB1 monooxygenase activity. J. Biochem. Toxicol. 4:1989;1-6
    • (1989) J. Biochem. Toxicol. , vol.4 , pp. 1-6
    • Platt, K.L.1    Molitor, E.2    Dohemer, J.3    Dogra, S.4    Oesch, F.5
  • 45
    • 0034534895 scopus 로고    scopus 로고
    • Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions
    • Ritter J.K. Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions. Chem. Biol. Interact. 129:2000;171-193
    • (2000) Chem. Biol. Interact. , vol.129 , pp. 171-193
    • Ritter, J.K.1
  • 46
    • 0031238644 scopus 로고    scopus 로고
    • Purification and characterization of a cytochrome P450 from liver microsomes of Xenopus laevis
    • Saito H., Ohi H., Sugata E., Murayama N., Fujita Y., Higuchi S. Purification and characterization of a cytochrome P450 from liver microsomes of Xenopus laevis. Arch. Biochem. Biophys. 345:1997;56-64
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 56-64
    • Saito, H.1    Ohi, H.2    Sugata, E.3    Murayama, N.4    Fujita, Y.5    Higuchi, S.6
  • 48
    • 0020006613 scopus 로고
    • Hepatic cytochrome P450-dependent monooxygenase systems of the trout, frog and snake-III. Induction
    • Schwen R.J., Mannering G.J. Hepatic cytochrome P450-dependent monooxygenase systems of the trout, frog and snake-III. Induction. Comp. Biochem. Physiol. 71B:1982;445-453
    • (1982) Comp. Biochem. Physiol. , vol.71 , pp. 445-453
    • Schwen, R.J.1    Mannering, G.J.2
  • 49
    • 0027179792 scopus 로고
    • Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozotocin-induced diabetes
    • Shimojio N., Ishizaki T., Imaoka S., Funae Y., Fujii S., Okuda K. Changes in amounts of cytochrome P450 isozymes and levels of catalytic activities in hepatic and renal microsomes of rats with streptozotocin-induced diabetes. Biochem. Pharmacol. 46:1993;621-627
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 621-627
    • Shimojio, N.1    Ishizaki, T.2    Imaoka, S.3    Funae, Y.4    Fujii, S.5    Okuda, K.6
  • 50
    • 85053290947 scopus 로고
    • Biochemistry and molecular biology of monooxygenases: Current perspectives on farms, functions and regulation of cytochrome P-450 in aquatic species
    • Malins, D.C., Ostrander, G.K. (Eds.), CRC Press, Ann Arbor
    • Stegeman, J.J., Hahn, M.E., 1994. Biochemistry and molecular biology of monooxygenases: current perspectives on farms, functions and regulation of cytochrome P-450 in aquatic species. In: Malins, D.C., Ostrander, G.K. (Eds.), Aquatic Toxicology. Molecular, Biochemical and Cellular Perspectives. CRC Press, Ann Arbor, pp. 87-206.
    • (1994) Aquatic Toxicology. Molecular, Biochemical and Cellular Perspectives , pp. 87-206
    • Stegeman, J.J.1    Hahn, M.E.2
  • 51
    • 0030679602 scopus 로고    scopus 로고
    • Metabolic capacity of nasal tissue interspecies comparisons of xenobiotic-metabolizing enzymes
    • Thornton-Manning J.R., Dahl A.R. Metabolic capacity of nasal tissue interspecies comparisons of xenobiotic-metabolizing enzymes. Mutat. Res. 380:1997;43-59
    • (1997) Mutat. Res. , vol.380 , pp. 43-59
    • Thornton-Manning, J.R.1    Dahl, A.R.2
  • 52
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Stachelin P., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stachelin, P.2    Gordon, J.3
  • 53
    • 0027139782 scopus 로고
    • Enzyme-kinetic and immunochemical characteristics of mouse cDNA-expressed, microsomal and purified CYP1A1 and CYP1A2
    • Tsyrlov I.B., Goldfarb I.S., Gelboin H.V. Enzyme-kinetic and immunochemical characteristics of mouse cDNA-expressed, microsomal and purified CYP1A1 and CYP1A2. Arch. Biochem. Biophys. 307:1993;259-266
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 259-266
    • Tsyrlov, I.B.1    Goldfarb, I.S.2    Gelboin, H.V.3
  • 54
    • 0020664888 scopus 로고
    • High-affinity nitrosamine dealkylase system in rat liver microsomes and its induction by fasting
    • Tu Y.Y., Yang C.S. High-affinity nitrosamine dealkylase system in rat liver microsomes and its induction by fasting. Cancer Res. 43:1983;623-629
    • (1983) Cancer Res. , vol.43 , pp. 623-629
    • Tu, Y.Y.1    Yang, C.S.2
  • 55
    • 0034534421 scopus 로고    scopus 로고
    • Glutathione conjugation as a bioactivation reaction
    • Van Bladeren P.J. Glutathione conjugation as a bioactivation reaction. Chem. Biol. Int. 129:2000;61-76
    • (2000) Chem. Biol. Int. , vol.129 , pp. 61-76
    • Van Bladeren, P.J.1
  • 56
    • 0027225741 scopus 로고
    • Olfactory cytochrome P-450 immunoreactivity in mice is altered by dichlobenil but preserved by metyrapone
    • Walters E., Buchheit K., Maruniak J.A. Olfactory cytochrome P-450 immunoreactivity in mice is altered by dichlobenil but preserved by metyrapone. Toxicology. 81:1993;113-122
    • (1993) Toxicology , vol.81 , pp. 113-122
    • Walters, E.1    Buchheit, K.2    Maruniak, J.A.3
  • 58
    • 0022518591 scopus 로고
    • Carbonyl reductase provides the enzymatic basis of quinone detoxication in man
    • Wermuth B., Platt K.L., Scidel A., Oesch F. Carbonyl reductase provides the enzymatic basis of quinone detoxication in man. Biochem. Pharmacol. 35:1986;1277-1282
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1277-1282
    • Wermuth, B.1    Platt, K.L.2    Scidel, A.3    Oesch, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.