메뉴 건너뛰기




Volumn 22, Issue 1, 1997, Pages 45-56

Molecular cloning of mouse liver flavin containing monooxygenase (FMO1) cDNA and characterization of the expression product: Metabolism of the neurotoxin, 1,2,3,4-tetrahydroisoquinoline (TIQ)

Author keywords

1,2,3,4 Tetrahydroisoquinoline; Flavin containing monooxygenase; Mouse liver; Neurotoxin; Yeast

Indexed keywords

CHLORPROMAZINE; DIMETHYLHYDRAZINE; IMIPRAMINE; N,N DIMETHYLANILINE; NEUROTOXIN; NICOTINE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROISOQUINOLINE; THIOACETAMIDE; THIOBENZAMIDE DERIVATIVE; THIOUREA; TRIMETHYLAMINE; UNSPECIFIC MONOOXYGENASE;

EID: 0030985787     PISSN: 03881350     EISSN: 18803989     Source Type: Journal    
DOI: 10.2131/jts.22.45     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0020645051 scopus 로고
    • Academic Press, New York
    • Ammerer, G., (1983) : Methods Enzymol (Academic Press, New York) 101, 192-201.
    • (1983) Methods Enzymol , vol.101 , pp. 192-201
    • Ammerer, G.1
  • 2
    • 0027315840 scopus 로고
    • Cloning, se-quencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1
    • Atta-Asofo-Adjei, E., Lawton, M. P. and Philpot, R. M. (1993) : Cloning, se-quencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1, J. Biol. Chem., 268, 9681-9689
    • (1993) J. Biol. Chem. , vol.268 , pp. 9681-9689
    • Atta-Asofo-Adjei, E.1    Lawton, M.P.2    Philpot, R.M.3
  • 3
    • 0001496694 scopus 로고
    • A primate model of parkinsonism: Selective destruction of dopaminergic neurons in the pars conpacta of the substantia nigra by N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
    • Burns, R. S., Chiueh, C. C., Markey, S. P., Ebert, M. H., Jacobowitz, D. M. and Kopin, I. J. (1983) : A primate model of parkinsonism: selective destruction of dopaminergic neurons in the pars conpacta of the substantia nigra by N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, Proc. Natl. Acad. Sci. USA., 80, 4546-4550
    • (1983) Proc. Natl. Acad. Sci. USA. , vol.80 , pp. 4546-4550
    • Burns, R.S.1    Chiueh, C.C.2    Markey, S.P.3    Ebert, M.H.4    Jacobowitz, D.M.5    Kopin, I.J.6
  • 4
    • 0028279350 scopus 로고
    • Cloning and sequencing of flavin-containing monooxygenase FMO3 and FMO4 from rabbit and characterization of FMO3
    • Burnet V. L., Lawton, M. P. and Philpot, R. M. (1994) Cloning and sequencing of flavin-containing monooxygenase FMO3 and FMO4 from rabbit and characterization of FMO3, J. Biol. Chem., 269, 14314-14322.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14314-14322
    • Burnet, V.L.1    Lawton, M.P.2    Philpot, R.M.3
  • 5
    • 0022634053 scopus 로고
    • Contribution of N-oxygenation to the metabolism of MPTP (1-methyl-4-phenyl-1,2,3,6- Tetrahydropyridine) by various liver preparations
    • Cashman, J. R. and Ziegler, D. M. (1986) Contribution of N-oxygenation to the metabolism of MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) by various liver preparations, Mol. Pharmacol., 29, 163-167.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 163-167
    • Cashman, J.R.1    Ziegler, D.M.2
  • 6
    • 0018639079 scopus 로고
    • Identification of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., Przybyla, A. E., Macdonald, R. J. and Rutter, W. J. (1979) : Identification of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry, 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    Macdonald, R.J.3    Rutter, W.J.4
  • 7
    • 0020366526 scopus 로고
    • Immunochemical comparison and quantitation of microsomal flavin-containing monooxygenase in various hog, mouse, rat, rabbit, dog, and human tissues
    • Dannan, G. D. and Guengerich, F. P. (1982) Immunochemical comparison and quantitation of microsomal flavin-containing monooxygenase in various hog, mouse, rat, rabbit, dog, and human tissues, Mol. Pharmacol., 22, 787-794
    • (1982) Mol. Pharmacol. , vol.22 , pp. 787-794
    • Dannan, G.D.1    Guengerich, F.P.2
  • 9
    • 0026805954 scopus 로고
    • Cloning, primary sequence and chro-mosomal localization of human FMO2, a new member of the flavin-containing monooxygenases
    • Dolphin, C. T., Shephard, E. A., Povey, S., Smith, R. L. and Phillips, I. R. (1992) : Cloning, primary sequence and chro-mosomal localization of human FMO2, a new member of the flavin-containing monooxygenases, Biochem. J., 287, 261-267.
    • (1992) Biochem. J. , vol.287 , pp. 261-267
    • Dolphin, C.T.1    Shephard, E.A.2    Povey, S.3    Smith, R.L.4    Phillips, I.R.5
  • 10
    • 0025129295 scopus 로고
    • The flavin-containing monooxygenase expressed in pig liver: Primary sequence, distribution, and evidence for a single gene
    • Gasser, R., Tynes, R. E., Lawton, M. P., Korsmeyer, K. K., Ziegler, D. M. and Philpot, R. M. (1990) The flavin-containing monooxygenase expressed in pig liver: primary sequence, distribution, and evidence for a single gene, Biochemistry, 29, 119-124.
    • (1990) Biochemistry , vol.29 , pp. 119-124
    • Gasser, R.1    Tynes, R.E.2    Lawton, M.P.3    Korsmeyer, K.K.4    Ziegler, D.M.5    Philpot, R.M.6
  • 12
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983) : Transformation of intact yeast cells treated with alkali cations, J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 13
    • 0027300958 scopus 로고
    • Rat liver flavin-containing monooxygenase (FMO): cDNA cloning and expression in yeast
    • Itoh, K., Kimura, T., Itoh, S. and Kamataki, T. (1993) : Rat liver flavin-containing monooxygenase (FMO): cDNA cloning and expression in yeast, Biochim. Biophys. Acta, 1173, 165-171.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 165-171
    • Itoh, K.1    Kimura, T.2    Itoh, S.3    Kamataki, T.4
  • 14
    • 0017258112 scopus 로고
    • Microsomal N-oxidation of the hepa-tocarcinogen N-methyl-4-aminoazobenzene and the reactivity of N-hydroxy-N-methyl-4-aminoazobenzene
    • Kadlubar, F. F. and Miller, E. C. (1976) : Microsomal N-oxidation of the hepa-tocarcinogen N-methyl-4-aminoazobenzene and the reactivity of N-hydroxy-N-methyl-4-aminoazobenzene, Cancer Res., 36, 1196-1206.
    • (1976) Cancer Res. , vol.36 , pp. 1196-1206
    • Kadlubar, F.F.1    Miller, E.C.2
  • 15
    • 0020033978 scopus 로고
    • N-Hydroxylation enzyme of carcinogenic aminoazo dyes: Possible involvement of cytochrome P-448
    • Kimura, T., Kodama, M. and Nagata, C. (1982) : N-Hydroxylation enzyme of carcinogenic aminoazo dyes: possible involvement of cytochrome P-448, Gann, 73, 55-62.
    • (1982) Gann , vol.73 , pp. 55-62
    • Kimura, T.1    Kodama, M.2    Nagata, C.3
  • 16
    • 0021113594 scopus 로고
    • Purification of mixed-function amine oxidase from rat liver microsome
    • Kimura, T., Kodama, M. and Nagata, C. (1983) : Purification of mixed-function amine oxidase from rat liver microsome, Biochem. Biophys. Res. Commun., 110, 640-645.
    • (1983) Biochem. Biophys. Res. Commun. , vol.110 , pp. 640-645
    • Kimura, T.1    Kodama, M.2    Nagata, C.3
  • 17
    • 0023011644 scopus 로고
    • Tetrahydroisoquinoline and 1-methylte-trahydroisoquinoline as novel endogenous amines in rat brain
    • Kohno, M., Ohta, S. and Hirobe, M. (1986) : Tetrahydroisoquinoline and 1-methylte-trahydroisoquinoline as novel endogenous amines in rat brain, Biochem. Biophys. Res. Commun., 140, 448-454
    • (1986) Biochem. Biophys. Res. Commun. , vol.140 , pp. 448-454
    • Kohno, M.1    Ohta, S.2    Hirobe, M.3
  • 18
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequence from 699 vertebrate messenger RNAs
    • Kozak, M. (1987) : An analysis of 5′-noncoding sequence from 699 vertebrate messenger RNAs, Nucl. Acids. Res., 15, 8125-8148.
    • (1987) Nucl. Acids. Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 19
    • 0024546509 scopus 로고
    • The sequencing model for translation: An update
    • Kozak, M. (1989) : The sequencing model for translation: an update, J. Cell. Biol., 108, 229-241.
    • (1989) J. Cell. Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 20
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidineanalog synthesis
    • Langston, J. W., Ballard, P., Tetrud, J. W. and Irwin, I. (1983) :Chronic parkinsonism in humans due to a product of meperidineanalog synthesis, Science, 219, 979-980
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 21
    • 0025219896 scopus 로고
    • The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes
    • Lawton, M. P., Gasser, R., Tynes, R. E., Hodgson, E. and Philpot, R. M. (1990) : The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes, J. Biol. Chem., 265, 5855-5861.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5855-5861
    • Lawton, M.P.1    Gasser, R.2    Tynes, R.E.3    Hodgson, E.4    Philpot, R.M.5
  • 23
    • 0026501232 scopus 로고
    • Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver
    • Lomri, N., Gu, Q. and Cashman, J. R. (1992) : Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver, Proc. Natl. Acad. Sci., U. S. A., 89, 1685-1689.
    • (1992) Proc. Natl. Acad. Sci., U. S. A. , vol.89 , pp. 1685-1689
    • Lomri, N.1    Gu, Q.2    Cashman, J.R.3
  • 25
    • 0025167615 scopus 로고
    • Confirmation of the enantiomers of 1-methyl-1,2,3,4-tetrahydroisoquinoline in the mouse brain and food applying gas chromatography/mass spectrometry with negative ion chemical ionization
    • Makio, Y., Tasaki, Y., Ohta, S. and Hirobe, M. (1990) : Confirmation of the enantiomers of 1-methyl-1,2,3,4-tetrahydroisoquinoline in the mouse brain and food applying gas chromatography/mass spectrometry with negative ion chemical ionization, Biomed. Environmental Mass Spectrometry, 19, 415-419
    • (1990) Biomed. Environmental Mass Spectrometry , vol.19 , pp. 415-419
    • Makio, Y.1    Tasaki, Y.2    Ohta, S.3    Hirobe, M.4
  • 26
    • 0026937248 scopus 로고
    • Guinea pig or rabbit lung flavin-containing monooxygenase with distinct mobilities in SDS-PAGE are Allelic variants that differ at only two positions
    • Nikbakht, K. N., Lawton, M. P. and Philpot, R. M. (1992) : Guinea pig or rabbit lung flavin-containing monooxygenase with distinct mobilities in SDS-PAGE are Allelic variants that differ at only two positions, Pharmacogenetics, 2, 207-216.
    • (1992) Pharmacogenetics , vol.2 , pp. 207-216
    • Nikbakht, K.N.1    Lawton, M.P.2    Philpot, R.M.3
  • 27
    • 0026060723 scopus 로고
    • Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes
    • McKie, J. H. and Douglas, K. T. (1991) : Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes, FEBS, 279, 5-8.
    • (1991) FEBS , vol.279 , pp. 5-8
    • McKie, J.H.1    Douglas, K.T.2
  • 28
    • 0023194188 scopus 로고
    • Presence of tetrahydroisoquinoline and 2-methyltetrahydroisoquinoline in parkinsonian and normal brain
    • Niwa, T., Takeda, N., Kaneda, N., Hashizume, Y. and Nagatsu, T. (1987) : Presence of tetrahydroisoquinoline and 2-methyltetrahydroisoquinoline in parkinsonian and normal brain,Biochem. Biophys. Res. Commun., 144, 1084-1089
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 1084-1089
    • Niwa, T.1    Takeda, N.2    Kaneda, N.3    Hashizume, Y.4    Nagatsu, T.5
  • 29
    • 0025740995 scopus 로고
    • Presence of 2-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroiso-quinoline and 1,2-dimethyl- 6,7-dihydroxytetrahydroisoquinoline, novel endogenous amine, in parkinsonian and normal human brains
    • Niwa, T., Takeda, N., Yoshizumi, H., Tatematu, A., Yoshida, M., Dostert, P., Naoi, M. and Nagatsu, T. (1991) : Presence of 2-methyl-6,7-dihydroxy-1,2,3,4-tetrahydroiso-quinoline and 1,2-dimethyl-6,7-dihydroxytetrahydroisoquinoline, novel endogenous amine, in parkinsonian and normal human brains, Biochem. Biophys. Res. Commun., 177, 603-609.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 603-609
    • Niwa, T.1    Takeda, N.2    Yoshizumi, H.3    Tatematu, A.4    Yoshida, M.5    Dostert, P.6    Naoi, M.7    Nagatsu, T.8
  • 30
    • 0023625261 scopus 로고
    • Tetrahydroisoquinoline and 1-methyltetrahydroisoquinoline are present in the human brain
    • Ohta, S., Kohno, M., Makino, Y., Tachikawa, O. and Hirobe, M. (1987) : Tetrahydroisoquinoline and 1-methyltetrahydroisoquinoline are present in the human brain, Biomed. Res., 8, 453-456
    • (1987) Biomed. Res. , vol.8 , pp. 453-456
    • Ohta, S.1    Kohno, M.2    Makino, Y.3    Tachikawa, O.4    Hirobe, M.5
  • 31
    • 0025302148 scopus 로고
    • Covalent structure of liver microsomal flavincontaining monooxygenase form 1
    • Ozols, J. (1990) : Covalent structure of liver microsomal flavincontaining monooxygenase form 1, J. Biol. Chem., 265, 10,289-10,299.
    • (1990) J. Biol. Chem. , vol.265 , Issue.10 , pp. 289-310
    • Ozols, J.1
  • 32
    • 0016259426 scopus 로고
    • S-Oxidation of thioureylenes catalyzed by a microsomal flavoprotein mixed-function oxidase
    • Poulsen, L. L., Hyslop, R. M. and Ziegler, D. M. (1974) : S-Oxidation of thioureylenes catalyzed by a microsomal flavoprotein mixed-function oxidase, Biochem. Pharmacol., 23, 3431-3440.
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 3431-3440
    • Poulsen, L.L.1    Hyslop, R.M.2    Ziegler, D.M.3
  • 33
    • 0018642835 scopus 로고
    • S-Oxygenation of N-substituted thioureas catalyzed by the pig liver microsomal FAD-containing monooxyge-nase
    • Poulsen, L. L., Hyslop, R. and Ziegler, D. M. (1979) S-Oxygenation of N-substituted thioureas catalyzed by the pig liver microsomal FAD-containing monooxyge-nase, Arch. Biochem. Biophys., 198, 78-88.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 78-88
    • Poulsen, L.L.1    Hyslop, R.2    Ziegler, D.M.3
  • 34
    • 0021190289 scopus 로고
    • Purification of the flavin-containing monooxygenase from mouse and pig liver microsomes
    • Sabourin, P. J., Smyser, B. P. and Hodgson, E. (1984) Purification of the flavin-containing monooxygenase from mouse and pig liver microsomes, Int. J. Biochem., 16, 713-720.
    • (1984) Int. J. Biochem. , vol.16 , pp. 713-720
    • Sabourin, P.J.1    Smyser, B.P.2    Hodgson, E.3
  • 36
    • 0022254395 scopus 로고
    • Metabolism of phosphorus-containing compounds by pig liver microsomal FAD containing monooxygenase
    • Smyser, B. P. and Hodgson, E. (1985) : Metabolism of phosphorus-containing compounds by pig liver microsomal FAD containing monooxygenase, Biochem. Pharmacol., 34, 1145-1150.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1145-1150
    • Smyser, B.P.1    Hodgson, E.2
  • 37
    • 0018142289 scopus 로고
    • Microsomal mixed-function amine oxidase oxidation of piperidine-substituted phenothiazine drugs
    • Sofer, S.S. and Ziegler, D. M. (1978) : Microsomal mixed-function amine oxidase oxidation of piperidine-substituted phenothiazine drugs, Drug Metab. Dispos., 232-239.
    • (1978) Drug Metab. Dispos. , pp. 232-239
    • Sofer, S.S.1    Ziegler, D.M.2
  • 38
    • 0025718695 scopus 로고
    • 1-Methyl-1,2,3,4-tetrahydroiso-quinoline, decreasing in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-treated mouse, prevents parkinsonism-like behavior abnormalities
    • Tasaki, Y., Makino, Y., Ohta, S. and Hirobe, M. (1991) : 1-Methyl-1,2,3,4-tetrahydroiso-quinoline, decreasing in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-treated mouse, prevents parkinsonism-like behavior abnormalities, J. Neurochem., 57, 1940-1943
    • (1991) J. Neurochem. , vol.57 , pp. 1940-1943
    • Tasaki, Y.1    Makino, Y.2    Ohta, S.3    Hirobe, M.4
  • 39
    • 0021857974 scopus 로고
    • Catalytic activity of substrate specificity of the flavin-containing monooxygenase in microsomal systems: Characterization of the hepatic, pulmonary and renal enzymes of the mouse, rabbit and rat
    • Tynes, R. E. and Hodgson, E. (1985) Catalytic activity of substrate specificity of the flavin-containing monooxygenase in microsomal systems: characterization of the hepatic, pulmonary and renal enzymes of the mouse, rabbit and rat, Arch. Biochem. Biophys., 240, 77-93.
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 77-93
    • Tynes, R.E.1    Hodgson, E.2
  • 40
    • 0020627843 scopus 로고
    • Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant
    • Wierenga, R. K. and Hol, W. G. J. (1983) : Predicted nucleotide-binding properties of p21 protein and its cancer-associated variant, Nature, 302, 842-844.
    • (1983) Nature , vol.302 , pp. 842-844
    • Wierenga, R.K.1    Hol, W.G.J.2
  • 41
    • 0004726189 scopus 로고
    • (Li, P. C. H.ed.), Academic Press, New York
    • Winzler, R. J. (1972) : In Hormone Proteins and Peptides, (Li, P. C. H.ed.), pp1-15., Academic Press, New York.
    • (1972) Hormone Proteins and Peptides , pp. 1-15
    • Winzler, R.J.1
  • 42
    • 0021747810 scopus 로고
    • Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme
    • Williams, D. E., Ziegler, D. M., Nordin, D. J., Hale, S. E. and Masters, B. S. S. (1985) : Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme, Biochem. Biophys. Res. Commun., 125, 116-122.
    • (1985) Biochem. Biophys. Res. Commun. , vol.125 , pp. 116-122
    • Williams, D.E.1    Ziegler, D.M.2    Nordin, D.J.3    Hale, S.E.4    Masters, B.S.S.5
  • 43
    • 0022360477 scopus 로고
    • Rabbit lung flavin-containing monooxygenase: Purification, characterization, and induction during pregnancy
    • Williams, D. E., Hale, S. E., Muerhoff, A. S. and Masters, B. S. S. (1985) : Rabbit lung flavin-containing monooxygenase: purification, characterization, and induction during pregnancy, Mol. Pharmacol., 28, 381-390.
    • (1985) Mol. Pharmacol. , vol.28 , pp. 381-390
    • Williams, D.E.1    Hale, S.E.2    Muerhoff, A.S.3    Masters, B.S.S.4
  • 44
    • 0026471565 scopus 로고
    • Neurotoxin: 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine,1,2,3,4-tetrahydro-isoquinoline and 1-methyl-6,7-dihydroxyte-trahydro-isoquinoline as substrates for FAD-containing monooxygenase of porcine liver microsomes
    • Wu, R. F., Miura, S. and Ichikawa, Y. (1992) : Neurotoxin: 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine,1,2,3,4-tetrahydro-isoquinoline and 1-methyl-6,7-dihydroxyte-trahydro-isoquinoline as substrates for FAD-containing monooxygenase of porcine liver microsomes, Biochem. Pharmacol., 44, 2079-2081
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 2079-2081
    • Wu, R.F.1    Miura, S.2    Ichikawa, Y.3
  • 45
    • 0028033728 scopus 로고
    • Characteristic properties and kinetic analysis with neurotoxins of porcine FAD-containing monooxygenase
    • Wu, R. F., Miura, S. and Ichikawa, Y. (1994) : Characteristic properties and kinetic analysis with neurotoxins of porcine FAD-containing monooxygenase, Biochim. Biophys. Acta., 1208, 204-210
    • (1994) Biochim. Biophys. Acta. , vol.1208 , pp. 204-210
    • Wu, R.F.1    Miura, S.2    Ichikawa, Y.3
  • 46
    • 0024993985 scopus 로고
    • Parkinsonism in monkeys produced by chronic administration of an endogenous substance of the brain, tetrahy-droisoquinoline: The behavioral and biochemical changes
    • Yoshida, M., Niwa, T. and Nagatsu, T. (1990) Parkinsonism in monkeys produced by chronic administration of an endogenous substance of the brain, tetrahy-droisoquinoline: the behavioral and biochemical changes, Neurosci. Lett., 119, 109-113
    • (1990) Neurosci. Lett. , vol.119 , pp. 109-113
    • Yoshida, M.1    Niwa, T.2    Nagatsu, T.3
  • 47
    • 1842282831 scopus 로고
    • Properties of a purifide microsomal mixed-function amine oxidase
    • (Kamin, H. ed.), University Park Press, Baltimore, MD
    • Ziegler, D. M., Jollow, D. and Cook, D. (1971): Properties of a purifide microsomal mixed-function amine oxidase, In Flavins and Flavoproteins, (Kamin, H. ed.), pp504-522. University Park Press, Baltimore, MD
    • (1971) Flavins and Flavoproteins , pp. 504-522
    • Ziegler, D.M.1    Jollow, D.2    Cook, D.3
  • 48
    • 0015337668 scopus 로고
    • Microsomal oxidase IV: Properties of a mixed-function amine oxidase isolated from pig liver microsomes
    • Ziegler, D. M. and Mitchell, C. H. (1972) : Microsomal oxidase IV: properties of a mixed-function amine oxidase isolated from pig liver microsomes, Arch. Biochem. Biophys., 150, 116-125.
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 116-125
    • Ziegler, D.M.1    Mitchell, C.H.2
  • 49
    • 0001440167 scopus 로고
    • Microsomal flavin-containing monooxygenase: Oxygenation of nucleophilic nitrogen and sulfur compounds
    • (Jakoby, W. B.ed.), Academic Press, New York
    • Ziegler, D. M. (1980) : Microsomal flavin-containing monooxygenase: Oxygenation of nucleophilic nitrogen and sulfur compounds, In Enzymatic Basis of Detoxication (Jakoby, W. B.ed.),vol. 1, pp201-225. Academic Press, New York.
    • (1980) Enzymatic Basis of Detoxication , vol.1 , pp. 201-225
    • Ziegler, D.M.1
  • 50
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenase : Catalytic mechanism and substrate specificities
    • Ziegler, D. M. (1988) : Flavin-containing monooxygenase : catalytic mechanism and substrate specificities, Drug Metab. Rev., 19, 1-32.
    • (1988) Drug Metab. Rev. , vol.19 , pp. 1-32
    • Ziegler, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.