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Volumn 26, Issue 3, 1998, Pages 284-287

Shorth communication: Expression of two different FMOs in sheep liver

Author keywords

[No Author keywords available]

Indexed keywords

ALBENDAZOLE; ANTISERUM; CYTOCHROME P450; MICROSOME ENZYME; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIAMAZOLE; TRIMETHYLAMINE; DIMETHYLANILINE MONOOXYGENASE; DIMETHYLANILINE MONOOXYGENASE (N-OXIDE FORMING); DRUG DERIVATIVE; IMIPRAMINE; METHIONINE; METHIONINE SULFOXIDE; METHYLAMINE; OXYGENASE;

EID: 0032015189     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0001440167 scopus 로고
    • Microsomal flavin-containing monooxygenase; oxygenation of nuleophilic nitrogen and sulfur compound
    • Jakoby WB ed Academic Press, New York
    • Ziegler DM (1980) Microsomal flavin-containing monooxygenase; oxygenation of nuleophilic nitrogen and sulfur compound. In Enzymatic basis of detoxification (Jakoby WB ed) Pp. 201-227, Academic Press, New York.
    • (1980) Enzymatic Basis of Detoxification , pp. 201-227
    • Ziegler, D.M.1
  • 2
    • 0023156080 scopus 로고
    • Trimethylaminuria (fish-odour-syndrome); an inborn error of oxidative metabolism
    • Waiz MA, Ayezh R, Mitchell SC, Idle JR and Smith RL (1987) Trimethylaminuria (fish-odour-syndrome); an inborn error of oxidative metabolism. Lancet 1:634-635.
    • (1987) Lancet , vol.1 , pp. 634-635
    • Waiz, M.A.1    Ayezh, R.2    Mitchell, S.C.3    Idle, J.R.4    Smith, R.L.5
  • 3
    • 0028245447 scopus 로고
    • Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes
    • Duescher RJ, Lawton MP, Philpot RM and Elfarra AA (1994) Flavin-containing monooxygenase (FMO)-dependent metabolism of methionine and evidence for FMO3 being the major FMO involved in methionine sulfoxidation in rabbit liver and kidney microsomes. J Biol Chem 269:17525-17530.
    • (1994) J Biol Chem , vol.269 , pp. 17525-17530
    • Duescher, R.J.1    Lawton, M.P.2    Philpot, R.M.3    Elfarra, A.A.4
  • 4
    • 0030249888 scopus 로고    scopus 로고
    • Characterization of the methionine S-oxidaze activity of rat liver and kidney for FMO3 being the major catalyst
    • Krause RJ, Ripp SL, Sausen PJ, Overby LH, Philpot RM and Elfarra AA (1996) Characterization of the methionine S-oxidaze activity of rat liver and kidney for FMO3 being the major catalyst. Arch Biochem Biophys 333:109-116.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 109-116
    • Krause, R.J.1    Ripp, S.L.2    Sausen, P.J.3    Overby, L.H.4    Philpot, R.M.5    Elfarra, A.A.6
  • 6
    • 0028265810 scopus 로고
    • The mammalian flavin-containing monooxygenases: Molecular characterization and regulation of expression
    • Hines RN, Cashman JR, Philpot RM, Williams DE and Ziegler DM (1993) The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression. Tox Appl Pharm 125:1-6.
    • (1993) Tox Appl Pharm , vol.125 , pp. 1-6
    • Hines, R.N.1    Cashman, J.R.2    Philpot, R.M.3    Williams, D.E.4    Ziegler, D.M.5
  • 7
    • 0015337668 scopus 로고
    • Microsomal oxydase IV: Properties of a mixed-function amine oxidase isolated from pig liver microsomes
    • Ziegler DM and Mitchell SC (1972) Microsomal oxydase IV: properties of a mixed-function amine oxidase isolated from pig liver microsomes. Arch Biophys Biochem 150:116-125.
    • (1972) Arch Biophys Biochem , vol.150 , pp. 116-125
    • Ziegler, D.M.1    Mitchell, S.C.2
  • 8
    • 0024435718 scopus 로고
    • 2 terminal segments homologous to the flavin containing NADPH monooxygenase of Pseudomonas fluorescence
    • 2 terminal segments homologous to the flavin containing NADPH monooxygenase of Pseudomonas fluorescence. Biochem Biophys Res Commun 163:49-55.
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 49-55
    • Ozols, J.1
  • 9
    • 0028280415 scopus 로고
    • Isolation and structure of a third form of liver microsomal flavin monooxygenase
    • Ozols J (1994) Isolation and structure of a third form of liver microsomal flavin monooxygenase. Biochemistry 33:3751-3757.
    • (1994) Biochemistry , vol.33 , pp. 3751-3757
    • Ozols, J.1
  • 10
    • 0028945438 scopus 로고
    • Structural and catalytic properties of the mammalian flavin-containing monooxygenase
    • Cashman JR (1995) Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem Res Toxicol 8:165-181.
    • (1995) Chem Res Toxicol , vol.8 , pp. 165-181
    • Cashman, J.R.1
  • 11
    • 0026501232 scopus 로고
    • Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver
    • Lomri N, Gu Q and Cashman JR (1992) Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. Proc Natl Acad Sci USA 89:1685-1689.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1685-1689
    • Lomri, N.1    Gu, Q.2    Cashman, J.R.3
  • 12
    • 0029149495 scopus 로고
    • The flavin-containing monooxygenases in rat liver: Evidence for the expression of a second form different from FMO1
    • Moroni P, Longin-Sauvageon C and Benoit E (1995a) The flavin-containing monooxygenases in rat liver: evidence for the expression of a second form different from FMO1. Biochem Biophys Res Commun 212:820-826.
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 820-826
    • Moroni, P.1    Longin-Sauvageon, C.2    Benoit, E.3
  • 13
    • 0022592940 scopus 로고
    • In vitro sulfoxidation of albendazole by ovine liver microsomes: Assay and frequency of various xenobiotics
    • Galtier P, Alvinerie M and Delatour P (1986) In vitro sulfoxidation of albendazole by ovine liver microsomes: assay and frequency of various xenobiotics. Am J Vet Res 47:447-452.
    • (1986) Am J Vet Res , vol.47 , pp. 447-452
    • Galtier, P.1    Alvinerie, M.2    Delatour, P.3
  • 14
    • 0028812229 scopus 로고
    • Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes
    • Moroni P, Buronfosse T, Longin-Sauvageon C, Delatour P and Benoit E (1995b) Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes. Drug Metab Dispos 23:160-165.
    • (1995) Drug Metab Dispos , vol.23 , pp. 160-165
    • Moroni, P.1    Buronfosse, T.2    Longin-Sauvageon, C.3    Delatour, P.4    Benoit, E.5
  • 15
    • 0024306127 scopus 로고
    • Distinct pulmonary and hepatic forms of flavin-containing in sheep
    • Williams DE, Meyers HH and Dutchuck MS (1989) Distinct pulmonary and hepatic forms of flavin-containing in sheep. Comp Biochem Physiol 938:465-470.
    • (1989) Comp Biochem Physiol , vol.938 , pp. 465-470
    • Williams, D.E.1    Meyers, H.H.2    Dutchuck, M.S.3
  • 16
    • 0021141593 scopus 로고
    • Spectrophotometric assay of the flavin-containing monooxygenase and changes in its activity in female mouse liver with nutritional and diurnal conditions
    • Dixit A and Roche TE (1984) Spectrophotometric assay of the flavin-containing monooxygenase and changes in its activity in female mouse liver with nutritional and diurnal conditions. Arch Biochem Biophys 223:50-63.
    • (1984) Arch Biochem Biophys , vol.223 , pp. 50-63
    • Dixit, A.1    Roche, T.E.2
  • 18
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford MA (1976) A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.A.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Stahelin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 89:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.89 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 21
    • 0001136317 scopus 로고
    • Algorithms for the solution of the nonlinear least-squares problems.nal
    • Gill PE and Murray W (1978) Algorithms for the solution of the nonlinear least-squares problems.nal. SIAM J Numer Anal 15:977-992.
    • (1978) SIAM J Numer Anal , vol.15 , pp. 977-992
    • Gill, P.E.1    Murray, W.2
  • 23
    • 0025181827 scopus 로고
    • Evidence for the presence of distinct favin-containing monooxygenases in human tissues
    • Lemoine A, Johan M and Cresteil T ( 1990) Evidence for the presence of distinct favin-containing monooxygenases in human tissues. Arch Biochem Biophys 276:336-342.
    • (1990) Arch Biochem Biophys , vol.276 , pp. 336-342
    • Lemoine, A.1    Johan, M.2    Cresteil, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.