메뉴 건너뛰기




Volumn 240, Issue 1-2, 2007, Pages 25-37

Inducibility of AhR-regulated CYP genes by β-naphthoflavone in the liver, lung, kidney and heart of the pig

Author keywords

AhR regulated CYPs; CYP 1A1 1A2 activity; Lung and heart; Pig liver

Indexed keywords

17BETA ESTRADIOL 4 HYDROXYLASE; 7 ETHOXY 4 TRIFLUOROMETHYLCOUMARIN; 7 ETHOXYCOUMARIN; 7 METHOXYRESORUFIN DEMETHYLASE; AROMATIC HYDROCARBON RECEPTOR; BETA NAPHTHOFLAVONE; BIOLOGICAL MARKER; CYTOCHROME P450; CYTOCHROME P450 1A1; CYTOCHROME P450 1A2; CYTOCHROME P450 1B1; ETHOXYRESORUFIN DEETHYLASE; GENE PRODUCT; ISOENZYME; MESSENGER RNA; METHYLTRANSFERASE; OXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 34548849104     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2007.07.015     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 0026742183 scopus 로고
    • Caffeine demethylase activity in human and dark agouti rat liver microsomes
    • Agundez J.A.G., Luengo A., and Benitez J. Caffeine demethylase activity in human and dark agouti rat liver microsomes. Drug Metab. Dispos. 20 (1992) 343-349
    • (1992) Drug Metab. Dispos. , vol.20 , pp. 343-349
    • Agundez, J.A.G.1    Luengo, A.2    Benitez, J.3
  • 2
    • 0029680494 scopus 로고    scopus 로고
    • Microsomal oxidation of N,N-diethylformamide and its effect on P450-dependent monooxygenases in rat liver
    • Amato G., Longo V., Mazzaccaro A., and Gervasi P.G. Microsomal oxidation of N,N-diethylformamide and its effect on P450-dependent monooxygenases in rat liver. Chem. Res. Toxicol. 9 (1996) 882-890
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 882-890
    • Amato, G.1    Longo, V.2    Mazzaccaro, A.3    Gervasi, P.G.4
  • 4
    • 0033858044 scopus 로고    scopus 로고
    • Effects of chlorinated hydrocarbons on expression of cytochrome P450 1A1, 1A2 and 1B1 and 2- and 4-hydroxylation of 17β-estradiol in female Sprague-Dawley
    • Badawi A., Cavalieri E., and Rogann E. Effects of chlorinated hydrocarbons on expression of cytochrome P450 1A1, 1A2 and 1B1 and 2- and 4-hydroxylation of 17β-estradiol in female Sprague-Dawley. Carcinogenesis 21 (2000) 1593-1599
    • (2000) Carcinogenesis , vol.21 , pp. 1593-1599
    • Badawi, A.1    Cavalieri, E.2    Rogann, E.3
  • 7
    • 0034454016 scopus 로고    scopus 로고
    • Determining the best animal model for human cytochrome P450 activities: a comparison of mouse, rat, rabbit, dog, micropig, monkey and man
    • Bogaards J.J.P., Bertrand M., Jackson P., Oudshoorn M.J., Weaver R.J., van Bladeren P.J., and Walther B. Determining the best animal model for human cytochrome P450 activities: a comparison of mouse, rat, rabbit, dog, micropig, monkey and man. Xenobiotica 30 (2000) 1131-1152
    • (2000) Xenobiotica , vol.30 , pp. 1131-1152
    • Bogaards, J.J.P.1    Bertrand, M.2    Jackson, P.3    Oudshoorn, M.J.4    Weaver, R.J.5    van Bladeren, P.J.6    Walther, B.7
  • 9
    • 14844365200 scopus 로고    scopus 로고
    • CAR and PXR expression and inducibility of CYP 2B and CYP 3A activities in rat and rabbit lungs
    • Chirulli V., Longo V., Marini S., Mazzaccaro A., Fiorio R., and Gervasi P.G. CAR and PXR expression and inducibility of CYP 2B and CYP 3A activities in rat and rabbit lungs. Life Sci. 76 (2005) 2535-2546
    • (2005) Life Sci. , vol.76 , pp. 2535-2546
    • Chirulli, V.1    Longo, V.2    Marini, S.3    Mazzaccaro, A.4    Fiorio, R.5    Gervasi, P.G.6
  • 10
    • 0023448111 scopus 로고
    • Expression and function of three cytochrome P450 isozymes in rat extrahepatic tissues
    • Christou M., Wilson N.M., and Jefcolate C.R. Expression and function of three cytochrome P450 isozymes in rat extrahepatic tissues. Arch. Biochem. Biophys. 258 (1987) 519-534
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 519-534
    • Christou, M.1    Wilson, N.M.2    Jefcolate, C.R.3
  • 11
    • 0030739223 scopus 로고    scopus 로고
    • Human cytochrome P4502B6 interindividual hepatic expression, substrate specificity and role in procarcinogen activation
    • Code R.S., Crespi C.L., Penman B.W., Gonzalez F.J., Chang T.K.H., and Waxman D.J. Human cytochrome P4502B6 interindividual hepatic expression, substrate specificity and role in procarcinogen activation. Drug Metab. Dispos. 25 (1997) 985-993
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 985-993
    • Code, R.S.1    Crespi, C.L.2    Penman, B.W.3    Gonzalez, F.J.4    Chang, T.K.H.5    Waxman, D.J.6
  • 13
    • 0033199820 scopus 로고    scopus 로고
    • Characterization of drug metabolizing activities in pig hepatocytes for use in bioartificial liver devices: comparison with other hepatic cellular models
    • Donato M.T., Castell J.V., and Gomez-Lechon M.J. Characterization of drug metabolizing activities in pig hepatocytes for use in bioartificial liver devices: comparison with other hepatic cellular models. J. Hepatol. 31 (1999) 542-549
    • (1999) J. Hepatol. , vol.31 , pp. 542-549
    • Donato, M.T.1    Castell, J.V.2    Gomez-Lechon, M.J.3
  • 15
    • 0026537062 scopus 로고
    • Biotransformation of caffeine and Theophyline in mammalian cell lines genetically engineered for expression of single cytochrome P450 isoforms
    • Fuhr U., Doehmer J., Battula N., Wolfel C., Kudla C., Keita Y., and Staib A.H. Biotransformation of caffeine and Theophyline in mammalian cell lines genetically engineered for expression of single cytochrome P450 isoforms. Biochem. Pharmacol. 43 (1992) 225-235
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 225-235
    • Fuhr, U.1    Doehmer, J.2    Battula, N.3    Wolfel, C.4    Kudla, C.5    Keita, Y.6    Staib, A.H.7
  • 16
    • 0001224244 scopus 로고    scopus 로고
    • Microtiter plate-based assay for rapid determination of enzyme activities of 13 P-450 supersomes and human liver microsomes
    • Ghosal A., Hapangama N., Yuan Y., Favreau L.V., Palamanda J.R., Partick J.E., Cayen M.N., and Zbaida S. Microtiter plate-based assay for rapid determination of enzyme activities of 13 P-450 supersomes and human liver microsomes. Drug Metab. Rev. 32 (2000) 188-199
    • (2000) Drug Metab. Rev. , vol.32 , pp. 188-199
    • Ghosal, A.1    Hapangama, N.2    Yuan, Y.3    Favreau, L.V.4    Palamanda, J.R.5    Partick, J.E.6    Cayen, M.N.7    Zbaida, S.8
  • 17
    • 0030735150 scopus 로고    scopus 로고
    • Comparison of catalytic selectivity of cytochrome P450 subfamily enzymes from different species
    • Guengerich F.P. Comparison of catalytic selectivity of cytochrome P450 subfamily enzymes from different species. Chem. Biol. Interact. 106 (1997) 161-182
    • (1997) Chem. Biol. Interact. , vol.106 , pp. 161-182
    • Guengerich, F.P.1
  • 18
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano P.R. (Ed), Kluwer Academic/Plenum Publishers, New York
    • Guengerich F.P. Human cytochrome P450 enzymes. In: Ortiz de Montellano P.R. (Ed). Cytochrome P450, Structure, Mechanism and Biochemistry. 3rd ed. (2005), Kluwer Academic/Plenum Publishers, New York 377-463
    • (2005) Cytochrome P450, Structure, Mechanism and Biochemistry. 3rd ed. , pp. 377-463
    • Guengerich, F.P.1
  • 19
    • 0034092954 scopus 로고    scopus 로고
    • Evidence for the catalysis of dextramethorphan-O-demethylation by a CYP2D6-like enzyme in pig liver
    • Jurima-Romet M., Casley W.L., Leblanc C.A., and Nowakowska M. Evidence for the catalysis of dextramethorphan-O-demethylation by a CYP2D6-like enzyme in pig liver. Toxicol. In Vitro 14 (2000) 253-263
    • (2000) Toxicol. In Vitro , vol.14 , pp. 253-263
    • Jurima-Romet, M.1    Casley, W.L.2    Leblanc, C.A.3    Nowakowska, M.4
  • 20
    • 0026451998 scopus 로고
    • Nature of cytochrome P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes
    • Kerlan V., Dreano Y., Bercovici J.P., Beaune P.H., Floch H.H., and Berthou F. Nature of cytochrome P450 involved in the 2-/4-hydroxylations of estradiol in human liver microsomes. Biochem. Pharmacol. 44 (1992) 1745-1756
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1745-1756
    • Kerlan, V.1    Dreano, Y.2    Bercovici, J.P.3    Beaune, P.H.4    Floch, H.H.5    Berthou, F.6
  • 22
    • 0036497073 scopus 로고    scopus 로고
    • Substrate specificity for rat cytochrome P450 (CYP) isoforms: screening with cDNA-expressed systems of the rat
    • Kobayashi K., Urashima K., Shimada N., and Chiba K. Substrate specificity for rat cytochrome P450 (CYP) isoforms: screening with cDNA-expressed systems of the rat. Biochem. Pharmacol. 63 (2002) 889-896
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 889-896
    • Kobayashi, K.1    Urashima, K.2    Shimada, N.3    Chiba, K.4
  • 23
    • 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
  • 24
    • 0034856688 scopus 로고    scopus 로고
    • Longterm stability of phase I and phase II enzymes of porcine liver cells in flat membrane biorectors
    • Langsch A., and Bader A. Longterm stability of phase I and phase II enzymes of porcine liver cells in flat membrane biorectors. Biotechnol. Bioeng. 76 (2001) 115-125
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 115-125
    • Langsch, A.1    Bader, A.2
  • 25
    • 0042315387 scopus 로고    scopus 로고
    • Characterization of the oxidative metabolites of 17β-estradiol and estrone formed by 15 selectively expressed human cytochrome P450 isoforms
    • Lee A.J., Cai M.X., Thomas P.E., Conney A.H., and Zhu B.T. Characterization of the oxidative metabolites of 17β-estradiol and estrone formed by 15 selectively expressed human cytochrome P450 isoforms. Endocrinology 144 (2003) 3382-3398
    • (2003) Endocrinology , vol.144 , pp. 3382-3398
    • Lee, A.J.1    Cai, M.X.2    Thomas, P.E.3    Conney, A.H.4    Zhu, B.T.5
  • 26
    • 0030036211 scopus 로고    scopus 로고
    • Molecular modelling of CYP1A subfamily members based on an alignment with CYP102: rationalitation of CYP1A substrate specificity in terms of active site aminoacid residues
    • Lewis D.F.V., and Lake B.G. Molecular modelling of CYP1A subfamily members based on an alignment with CYP102: rationalitation of CYP1A substrate specificity in terms of active site aminoacid residues. Xenobiotica 26 (1996) 723-753
    • (1996) Xenobiotica , vol.26 , pp. 723-753
    • Lewis, D.F.V.1    Lake, B.G.2
  • 27
    • 3843060093 scopus 로고    scopus 로고
    • Molecular cloning, expression and functional characterization of the cytochrome P450 2A6 gene in pig liver
    • Lin Z., Lou Y., and Squires E.J. Molecular cloning, expression and functional characterization of the cytochrome P450 2A6 gene in pig liver. Animal Gen. 35 (2004) 312-316
    • (2004) Animal Gen. , vol.35 , pp. 312-316
    • Lin, Z.1    Lou, Y.2    Squires, E.J.3
  • 28
    • 0026008585 scopus 로고
    • Role of cytochrome P450 1A2 in acetanilide 4-hydroxylation as determined with cDNA expression and monoclonal antibodies
    • Liu G., Gelboin H.V., and Myers M.J. Role of cytochrome P450 1A2 in acetanilide 4-hydroxylation as determined with cDNA expression and monoclonal antibodies. Arch. Biochem. Biophys. 284 (1991) 400-406
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 400-406
    • Liu, G.1    Gelboin, H.V.2    Myers, M.J.3
  • 29
    • 0026176952 scopus 로고
    • Drug metabolizing enzymes in liver, olfactory and respiratory epithelium of cattle
    • Longo V., Mazzaccaro A., Naldi F., and 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
  • 31
    • 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., and 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
  • 32
    • 0037090466 scopus 로고    scopus 로고
    • Cloning and expression of two novel pig liver and kidney fatty acid hydroxylases [cytochrome P450 (CYP)4A24 and CYP4A25]
    • Lundell K. Cloning and expression of two novel pig liver and kidney fatty acid hydroxylases [cytochrome P450 (CYP)4A24 and CYP4A25]. J. Biochem. 363 (2002) 297-303
    • (2002) J. Biochem. , vol.363 , pp. 297-303
    • Lundell, K.1
  • 33
    • 0031720849 scopus 로고    scopus 로고
    • Xenobiotic metabolizing enzymes in pig nasal and hepatic tissues
    • Marini S., Longo V., Mazzaccaro A., and Gervasi P.G. Xenobiotic metabolizing enzymes in pig nasal and hepatic tissues. Xenobiotica 10 (1998) 923-935
    • (1998) Xenobiotica , vol.10 , pp. 923-935
    • Marini, S.1    Longo, V.2    Mazzaccaro, A.3    Gervasi, P.G.4
  • 35
    • 0035006985 scopus 로고    scopus 로고
    • Identification of multiple constitutive and inducible hepatic cytochrome P450 enzymes in market weight swine
    • Myers M.J., Farrell D.E., Howard K.D., and Kawalek J.C. Identification of multiple constitutive and inducible hepatic cytochrome P450 enzymes in market weight swine. Drug Metab. Dispos. 29 (2001) 908-915
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 908-915
    • Myers, M.J.1    Farrell, D.E.2    Howard, K.D.3    Kawalek, J.C.4
  • 36
    • 17644389138 scopus 로고    scopus 로고
    • Characterization of adjacent E-Box and nuclear factor 1-like DNA binding sequence in the human CYP1A2 promoter
    • Narvaez M.J., Anderson G.R., Pickwell G.V., and Quattrocchi L.C. Characterization of adjacent E-Box and nuclear factor 1-like DNA binding sequence in the human CYP1A2 promoter. J. Biochem. Mol. Toxicol. 19 (2005) 78-86
    • (2005) J. Biochem. Mol. Toxicol. , vol.19 , pp. 78-86
    • Narvaez, M.J.1    Anderson, G.R.2    Pickwell, G.V.3    Quattrocchi, L.C.4
  • 37
    • 0033990325 scopus 로고    scopus 로고
    • Role of the aromatic hydrocarbon receptor and [Ah]gene battery in the oxidative stress response, cell cycle control and apoptosis
    • Nebert D.W., Roe A.L., Dieter M.Z., Solis W.A., Yang Y., and Dalton T.P. Role of the aromatic hydrocarbon receptor and [Ah]gene battery in the oxidative stress response, cell cycle control and apoptosis. Biochem. Pharmacol. 59 (2000) 65-85
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 65-85
    • Nebert, D.W.1    Roe, A.L.2    Dieter, M.Z.3    Solis, W.A.4    Yang, Y.5    Dalton, T.P.6
  • 38
    • 0041922374 scopus 로고    scopus 로고
    • Tissue distribution of mRNA expression of human cytochrome P450 isoforms assessed by high-sensitivity real-time reverse transcription PCR
    • Nishimura M., Yaguti H., Yoshitsugu H., Naito S., and Satoh T. Tissue distribution of mRNA expression of human cytochrome P450 isoforms assessed by high-sensitivity real-time reverse transcription PCR. Yakugaku Zasshi 123 (2003) 369-375
    • (2003) Yakugaku Zasshi , vol.123 , pp. 369-375
    • Nishimura, M.1    Yaguti, H.2    Yoshitsugu, H.3    Naito, S.4    Satoh, T.5
  • 39
    • 78651165715 scopus 로고
    • The carbon-monoxide binding protein of liver microsomes. I. Evidences for its hemoprotein nature
    • Omura T., and 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
  • 40
    • 0030056594 scopus 로고    scopus 로고
    • Specificity of substrate and inhibitor probes for cytochrome P450s: evaluation of in vitro metabolism using cDNA-expressed human P450s and human liver microsomes
    • Ono S., Hatanaka T., Hotta H., Satoh T., Gonzalez F.J., and Tsutsui M. Specificity of substrate and inhibitor probes for cytochrome P450s: evaluation of in vitro metabolism using cDNA-expressed human P450s and human liver microsomes. Xenobiotica 26 (1996) 681-693
    • (1996) Xenobiotica , vol.26 , pp. 681-693
    • Ono, S.1    Hatanaka, T.2    Hotta, H.3    Satoh, T.4    Gonzalez, F.J.5    Tsutsui, M.6
  • 41
    • 0025910053 scopus 로고
    • Characterization of pig liver purified cytochrome P-450 isoenzymes of ochratoxin A metabolism studies
    • Oster T., Jayyosi Z., Creppy E.E., el Amri H.S., and Batt A.M. Characterization of pig liver purified cytochrome P-450 isoenzymes of ochratoxin A metabolism studies. Toxicol. Lett. 57 (1991) 203-214
    • (1991) Toxicol. Lett. , vol.57 , pp. 203-214
    • Oster, T.1    Jayyosi, Z.2    Creppy, E.E.3    el Amri, H.S.4    Batt, A.M.5
  • 42
    • 0036016868 scopus 로고    scopus 로고
    • Induction of cytochrome P450 1A1 in multiple organs of minipigs after oral exposure to soils contaminated with polycyclic aromatic hydrocarbons (PAH)
    • Roos P.H., Tschirbs S., Welge P., Hack A., Theegarten D., Mogilevski G., and Vilhelm M. Induction of cytochrome P450 1A1 in multiple organs of minipigs after oral exposure to soils contaminated with polycyclic aromatic hydrocarbons (PAH). Arch. Toxicol. 76 (2002) 326-334
    • (2002) Arch. Toxicol. , vol.76 , pp. 326-334
    • Roos, P.H.1    Tschirbs, S.2    Welge, P.3    Hack, A.4    Theegarten, D.5    Mogilevski, G.6    Vilhelm, M.7
  • 43
    • 0025139447 scopus 로고
    • Purification and characterisation of hepatic microsomal cytochrome P450
    • Ryan D.E., and Levin W. Purification and characterisation of hepatic microsomal cytochrome P450. Pharmacol. Ther. 45 (1990) 153-239
    • (1990) Pharmacol. Ther. , vol.45 , pp. 153-239
    • Ryan, D.E.1    Levin, W.2
  • 44
    • 1842589311 scopus 로고    scopus 로고
    • Short communication: Cloning CYP2D21 and CYP3A22 cDNAs from liver of miniature pigs
    • Sakuma T., Shinojima T., Miwa K., and Kamataki T. Short communication: Cloning CYP2D21 and CYP3A22 cDNAs from liver of miniature pigs. Drug Metab. Dispos. 32 (2004) 376-378
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 376-378
    • Sakuma, T.1    Shinojima, T.2    Miwa, K.3    Kamataki, T.4
  • 46
    • 0036317196 scopus 로고    scopus 로고
    • Arylhydrocarbon receptor-dependent induction of liver and lung cytochromes P450 1A1, 1A2 and 1B1 by polycyclic aromatic hydrocarbons and polychlorinated biphenyls in genetically engineered C57BL/6J mice
    • Shimada T., Inoue K., Suzuki Y., Kawai T., Azuma E., Nakajima T., Shindo M., Kurose K., Sugie A., Yamagishi Y., Fujii Kuriyama Y., and Hashimoto M. Arylhydrocarbon receptor-dependent induction of liver and lung cytochromes P450 1A1, 1A2 and 1B1 by polycyclic aromatic hydrocarbons and polychlorinated biphenyls in genetically engineered C57BL/6J mice. Carcinogenesis 23 (2002) 1199-1207
    • (2002) Carcinogenesis , vol.23 , pp. 1199-1207
    • Shimada, T.1    Inoue, K.2    Suzuki, Y.3    Kawai, T.4    Azuma, E.5    Nakajima, T.6    Shindo, M.7    Kurose, K.8    Sugie, A.9    Yamagishi, Y.10    Fujii Kuriyama, Y.11    Hashimoto, M.12
  • 47
    • 0037440941 scopus 로고    scopus 로고
    • Tissue-specific induction of cytochromes P450 1A1 and 1B1 by polycyclic aromatic hydrocarbons and polychlorinated biphenyls in engineered C57BL/6J mice of arylhydrocarbon receptor gene
    • Shimada T., Sugie A., Shindo M., Nakajima T., Azuma E., Hashimoto M., and Inoue K. Tissue-specific induction of cytochromes P450 1A1 and 1B1 by polycyclic aromatic hydrocarbons and polychlorinated biphenyls in engineered C57BL/6J mice of arylhydrocarbon receptor gene. Toxicol. Appl. Pharmacol. 187 (2003) 1-10
    • (2003) Toxicol. Appl. Pharmacol. , vol.187 , pp. 1-10
    • Shimada, T.1    Sugie, A.2    Shindo, M.3    Nakajima, T.4    Azuma, E.5    Hashimoto, M.6    Inoue, K.7
  • 48
    • 0030760363 scopus 로고    scopus 로고
    • Characterization of the P450 system in Gottingen minipigs
    • Skaanild M.T., and Friis C. Characterization of the P450 system in Gottingen minipigs. Pharmacol. Toxicol. 80 (1997) 28-33
    • (1997) Pharmacol. Toxicol. , vol.80 , pp. 28-33
    • Skaanild, M.T.1    Friis, C.2
  • 51
    • 0025951974 scopus 로고
    • Purification and characterization of hepatic microsomal cytochrome P-450 in phenobarbital- and beta-naphthoflavone-treated pigs
    • Thomsen M.K., Friis C., and Nielsen P. Purification and characterization of hepatic microsomal cytochrome P-450 in phenobarbital- and beta-naphthoflavone-treated pigs. Pharmacol. Toxicol. 69 (1991) 381-385
    • (1991) Pharmacol. Toxicol. , vol.69 , pp. 381-385
    • Thomsen, M.K.1    Friis, C.2    Nielsen, P.3
  • 52
    • 0036793580 scopus 로고    scopus 로고
    • Testosterone, cytochrome P450 and cardiac hypertrophy
    • Thum T., and Borlak J. Testosterone, cytochrome P450 and cardiac hypertrophy. FASEB J. 16 (2002) 1537-1549
    • (2002) FASEB J. , vol.16 , pp. 1537-1549
    • Thum, T.1    Borlak, J.2
  • 53
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gel to nitrocellulose sheets: Procedure and some applications
    • Towbin H.T., Staehelin P., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gel to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehelin, P.2    Gordon, J.3
  • 54
    • 0027139782 scopus 로고
    • Enzyme-kinetic and immunochemical characteristics of mouse cDNA-expressed, microsomal and purified CYP1A1 and CYP1A2
    • Tsyrlov I.B., Goldfarb I.S., and 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
  • 55
    • 0031830896 scopus 로고    scopus 로고
    • Roles of cytochromes P450 1A2 and 3A4 in the oxidation of estradiol and estrone in human liver microsomes
    • Yamazaki H., Shaw P.M., Guengerich F.P., and Shimada T. Roles of cytochromes P450 1A2 and 3A4 in the oxidation of estradiol and estrone in human liver microsomes. Chem. Res. Toxicol. 11 (1998) 659-665
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 659-665
    • Yamazaki, H.1    Shaw, P.M.2    Guengerich, F.P.3    Shimada, T.4
  • 56
    • 0034090984 scopus 로고    scopus 로고
    • Human cytochrome P450 metabolism of retinals to retinoic acids
    • Zhang Q.Y., Dumbar D., and Kaminsky L. Human cytochrome P450 metabolism of retinals to retinoic acids. Drug Metab. Dispos. 29 (2000) 292-297
    • (2000) Drug Metab. Dispos. , vol.29 , pp. 292-297
    • Zhang, Q.Y.1    Dumbar, D.2    Kaminsky, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.