메뉴 건너뛰기




Volumn 121, Issue 1-3, 1998, Pages 185-195

Occurrence of flavin-containing monooxygenases in non-mammalian eukaryotic organisms

Author keywords

Bioactivation; Biotransformation; Evolution; Flavin containing monooxygenase; Osmoregulation; Trimethylamine

Indexed keywords

MESSENGER RNA; UNSPECIFIC MONOOXYGENASE; XENOBIOTIC AGENT;

EID: 0031738746     PISSN: 07428413     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0742-8413(98)10060-9     Document Type: Article
Times cited : (59)

References (63)
  • 1
    • 0023105353 scopus 로고
    • Conversion of N,N-dimethylaniline to N,N-dimethylaniline-N-oxide by a cytosolic flavin-containing enzyme from Trypanosoma cruzi
    • Agosin M., Ankley G.T. Conversion of N,N-dimethylaniline to N,N-dimethylaniline-N-oxide by a cytosolic flavin-containing enzyme from Trypanosoma cruzi. Drug Metab Dispos. 15:1987;200-203.
    • (1987) Drug Metab Dispos , vol.15 , pp. 200-203
    • Agosin, M.1    Ankley, G.T.2
  • 2
    • 0019877173 scopus 로고
    • Biosynthesis and turnover of trimethylamine oxide in the teleost cod, Gadus morhua
    • Agustsson I., Strom A.R. Biosynthesis and turnover of trimethylamine oxide in the teleost cod, Gadus morhua. J Biol Chem. 256:1981;8045-8049.
    • (1981) J Biol Chem , vol.256 , pp. 8045-8049
    • Agustsson, I.1    Strom, A.R.2
  • 3
    • 0025019238 scopus 로고
    • Genetic polymorphism of trimethylamine N-oxidation
    • Ayesh R., Smith R.L. Genetic polymorphism of trimethylamine N-oxidation. Pharmacol Ther. 45:1990;387-401.
    • (1990) Pharmacol Ther , vol.45 , pp. 387-401
    • Ayesh, R.1    Smith, R.L.2
  • 4
    • 0002598876 scopus 로고
    • A comparative study of trimethylamine-N-oxide biosynthesis
    • Baker J.R., Streuempler A., Chaykin S. A comparative study of trimethylamine-N-oxide biosynthesis. Biochim Biophys Acta. 71:1963;58-64.
    • (1963) Biochim Biophys Acta , vol.71 , pp. 58-64
    • Baker, J.R.1    Streuempler, A.2    Chaykin, S.3
  • 5
    • 0019876857 scopus 로고
    • The oxidative half-reaction of liver microsomal FAD-containing monooxygenase
    • Beaty N.B., Ballou D.P. The oxidative half-reaction of liver microsomal FAD-containing monooxygenase. J Biol Chem. 256:1981;4619-4625.
    • (1981) J Biol Chem , vol.256 , pp. 4619-4625
    • Beaty, N.B.1    Ballou, D.P.2
  • 6
    • 0022494236 scopus 로고
    • Selective activation of carcinogenic aromatic amines to bacterial mutagens in the marine mussel Mytilus galloprovincialis
    • Britvic S., Kurelec B. Selective activation of carcinogenic aromatic amines to bacterial mutagens in the marine mussel Mytilus galloprovincialis. Comp Biochem Physiol. 85C:1986;111-114.
    • (1986) Comp Biochem Physiol , vol.85 , pp. 111-114
    • Britvic, S.1    Kurelec, B.2
  • 7
    • 0024852297 scopus 로고
    • S-oxygenation of eptam in hepatic microsomes from fresh and saltwater striped bass (Morone saxatilis)
    • Cashman J.R., Olsen L.D. S-oxygenation of eptam in hepatic microsomes from fresh and saltwater striped bass (Morone saxatilis). Chem Res Toxicol. 2:1989;392-399.
    • (1989) Chem Res Toxicol , vol.2 , pp. 392-399
    • Cashman, J.R.1    Olsen, L.D.2
  • 8
    • 0025152139 scopus 로고
    • S-oxygenation of thiobencarb (bolero) in hepatic preparations from striped bass (Morone saxatilis) and mammalian systems
    • Cashman J.R., Olsen L.D., Nishioka R.S., Gray E.S., Bern H.A. S-oxygenation of thiobencarb (bolero) in hepatic preparations from striped bass (Morone saxatilis) and mammalian systems. Chem Res Toxicol. 3:1990;433-440.
    • (1990) Chem Res Toxicol , vol.3 , pp. 433-440
    • Cashman, J.R.1    Olsen, L.D.2    Nishioka, R.S.3    Gray, E.S.4    Bern, H.A.5
  • 9
    • 0029560984 scopus 로고
    • Oxidation of aldehydes catalyzed by pig liver flavin-containing monooxygenase
    • Chen G.P., Poulsen L.L., Ziegler D.M. Oxidation of aldehydes catalyzed by pig liver flavin-containing monooxygenase. Drug Metab Dispos. 23:1995;1390-1393.
    • (1995) Drug Metab Dispos , vol.23 , pp. 1390-1393
    • Chen, G.P.1    Poulsen, L.L.2    Ziegler, D.M.3
  • 10
    • 0345663864 scopus 로고
    • Changes in level of trimethylamine and trimethylamine oxide during adaptation of young eel Anguilla anguilla to a seawater environment
    • Daikoku T., Sakaguchi M. Changes in level of trimethylamine and trimethylamine oxide during adaptation of young eel Anguilla anguilla to a seawater environment. Nippon Suisan Gakkaishi. 56:1990;1895-1895.
    • (1990) Nippon Suisan Gakkaishi , vol.56 , pp. 1895-1895
    • Daikoku, T.1    Sakaguchi, M.2
  • 11
    • 45549119077 scopus 로고
    • Effects of intraperitoneally injected and dietary trimethylamine on the biosynthesis of trimethylamine oxide in relation to seawater adaptation of the eel Anguilla japonica and the guppy Poecilia reticulata
    • Daikoku T., Murata M., Sakaguchi M. Effects of intraperitoneally injected and dietary trimethylamine on the biosynthesis of trimethylamine oxide in relation to seawater adaptation of the eel Anguilla japonica and the guppy Poecilia reticulata. Comp Biochem Physiol. 89A:1988;261-264.
    • (1988) Comp Biochem Physiol , vol.89 , pp. 261-264
    • Daikoku, T.1    Murata, M.2    Sakaguchi, M.3
  • 12
    • 0026611401 scopus 로고
    • 35S-labeled thiocarbamides in rat liver microsomes
    • 35S-labeled thiocarbamides in rat liver microsomes. Biochem Pharmacol. 43:1992;881-888.
    • (1992) Biochem Pharmacol , vol.43 , pp. 881-888
    • Decker, C.J.1    Doerge, D.R.2
  • 13
    • 0023047651 scopus 로고
    • Mechanism-based inhibition of lactoperoxidase by thiocarbamide goitrogens
    • Doerge D.R. Mechanism-based inhibition of lactoperoxidase by thiocarbamide goitrogens. Biochemistry. 25:1986;4724-4728.
    • (1986) Biochemistry , vol.25 , pp. 4724-4728
    • Doerge, D.R.1
  • 14
    • 0031455166 scopus 로고    scopus 로고
    • The gene encoding flavin-containing monooxygenase 3 of man: Structural organization and identification of a mutation associated with the inherited disorder, fish odor syndrome
    • Dolphin C, Riley JH, Smith RL, Shephard EA, Phillips IR. The gene encoding flavin-containing monooxygenase 3 of man: Structural organization and identification of a mutation associated with the inherited disorder, fish odor syndrome. Genomics 1997;46:260-7.
    • (1997) Genomics , vol.46 , pp. 260-267
    • Dolphin, C.1    Riley, J.H.2    Smith, R.L.3    Shephard, E.A.4    Phillips, I.R.5
  • 15
    • 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 R.J., Lawton M.P., Philpot R.M., Elfarra A.A. 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. 269:1994;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
  • 16
    • 0015925799 scopus 로고
    • Trimethylamine oxidase of nurse shark liver and its relation to mammalian mixed function amine oxidase
    • Goldstein L., Dewitt-Harley S. Trimethylamine oxidase of nurse shark liver and its relation to mammalian mixed function amine oxidase. Comp Biochem Physiol. 45B:1973;895-903.
    • (1973) Comp Biochem Physiol , vol.45 , pp. 895-903
    • Goldstein, L.1    Dewitt-Harley, S.2
  • 17
    • 0016377815 scopus 로고
    • Trimethylamine oxide excretion rates in elasmobranchs
    • Goldstein L., Palatt P.J. Trimethylamine oxide excretion rates in elasmobranchs. Am J Physiol. 227:1974;1268-1272.
    • (1974) Am J Physiol , vol.227 , pp. 1268-1272
    • Goldstein, L.1    Palatt, P.J.2
  • 18
    • 0015924171 scopus 로고
    • Activities of ornithine-urea cycle enzymes and of trimethylamine oxidase in the coelacanth, Latimeria chalumnae
    • Goldstein L., Harley-Dewitt S., Forster R.F. Activities of ornithine-urea cycle enzymes and of trimethylamine oxidase in the coelacanth, Latimeria chalumnae. Comp Biochem Physiol. 44B:1973;357-362.
    • (1973) Comp Biochem Physiol , vol.44 , pp. 357-362
    • Goldstein, L.1    Harley-Dewitt, S.2    Forster, R.F.3
  • 20
    • 0022006601 scopus 로고
    • Metabolic oxidation of carcinogenic arylamines by rat, dog, and human hepatic microsomes and by purified flavin-containing and cytochrome P450 monooxygenases
    • Hammons G.J., Guengerich F.P., Weis C.C., Beland F.A., Kadlubar F.F. Metabolic oxidation of carcinogenic arylamines by rat, dog, and human hepatic microsomes and by purified flavin-containing and cytochrome P450 monooxygenases. Cancer Res. 45:1985;3578-3585.
    • (1985) Cancer Res , vol.45 , pp. 3578-3585
    • Hammons, G.J.1    Guengerich, F.P.2    Weis, C.C.3    Beland, F.A.4    Kadlubar, F.F.5
  • 21
    • 85008133989 scopus 로고
    • Trimethylamine oxide in fish muscle I. The origin of trimethylamine oxide in goldfish muscle
    • Hashimoto Y., Okaichi T. Trimethylamine oxide in fish muscle I. The origin of trimethylamine oxide in goldfish muscle. Bull Jap Soc Sci Fish. 24:1958;640-644.
    • (1958) Bull Jap Soc Sci Fish , vol.24 , pp. 640-644
    • Hashimoto, Y.1    Okaichi, T.2
  • 22
    • 85008112532 scopus 로고
    • Trimethylamine oxide in fish muscle II. Trimethylamine oxide in the muscle of eels kept in fresh and brackish water
    • Hashimoto Y., Okaichi T. Trimethylamine oxide in fish muscle II. Trimethylamine oxide in the muscle of eels kept in fresh and brackish water. Bull Jpn Soc Sci Fish. 24:1958;645-647.
    • (1958) Bull Jpn Soc Sci Fish , vol.24 , pp. 645-647
    • Hashimoto, Y.1    Okaichi, T.2
  • 24
    • 0028265810 scopus 로고
    • The mammalian flavin-containing monooxygenases: Molecular characterization and regulation of expression
    • Hines R.N., Cashman J.R., Philpot R.M., Williams D.E., Ziegler D.M. The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression. Toxicol Appl Pharmacol. 125:1994;1-6.
    • (1994) Toxicol Appl Pharmacol , 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
  • 25
    • 0022980412 scopus 로고
    • Reactions of the 4α-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates
    • Jones K.C., Ballou D.P. Reactions of the 4α-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J Biol Chem. 261:1986;2553-2559.
    • (1986) J Biol Chem , vol.261 , pp. 2553-2559
    • Jones, K.C.1    Ballou, D.P.2
  • 26
    • 0020578361 scopus 로고
    • Inhibition of the microsomal N-hydroxylation of 2-amino-6-nitrotoluene by a metabolite of methimazole
    • Kedderis G.L., Rickert D.E. Inhibition of the microsomal N-hydroxylation of 2-amino-6-nitrotoluene by a metabolite of methimazole. Biochem Biophys Res Commun. 113:1983;433-438.
    • (1983) Biochem Biophys Res Commun , vol.113 , pp. 433-438
    • Kedderis, G.L.1    Rickert, D.E.2
  • 27
    • 0021995799 scopus 로고
    • Loss of rat liver microsomal cytochrome P-450 during methimazole metabolism. Role of flavin-containing monooxygenase
    • Kedderis G.L., Rickert D.E. Loss of rat liver microsomal cytochrome P-450 during methimazole metabolism. Role of flavin-containing monooxygenase. Drug Metab Dispos. 13:1985;58-61.
    • (1985) Drug Metab Dispos , vol.13 , pp. 58-61
    • Kedderis, G.L.1    Rickert, D.E.2
  • 28
    • 0023610918 scopus 로고
    • Metabolic activation of 2-aminofluorene, 2-acetylaminofluorene and N-hydroxy-acetylaminofluorene to bacterial mutagens with mussel (Mytilus galloprovincialis) and carp (Cyprinus carpio) subcellular preparations
    • Kurelec B., Krca S. Metabolic activation of 2-aminofluorene, 2-acetylaminofluorene and N-hydroxy-acetylaminofluorene to bacterial mutagens with mussel (Mytilus galloprovincialis) and carp (Cyprinus carpio) subcellular preparations. Comp Biochem Physiol. 88C:1987;171-177.
    • (1987) Comp Biochem Physiol , vol.88 , pp. 171-177
    • Kurelec, B.1    Krca, S.2
  • 29
    • 0021792408 scopus 로고
    • Exclusive activation of aromatic amines in the marine mussel, Mytilus edulis by FAD-containing monooxygenase
    • Kurelec B. Exclusive activation of aromatic amines in the marine mussel, Mytilus edulis by FAD-containing monooxygenase. Biochem Biophys Res Commun. 126:1985;773-778.
    • (1985) Biochem Biophys Res Commun , vol.126 , pp. 773-778
    • Kurelec, B.1
  • 30
    • 0023142840 scopus 로고
    • Metabolism of some carcinogenic aromatic amines in four species of marine sponges
    • Kurelec B., Britvic S., Krca S., Muller W.E.G., Zahn R.K. Metabolism of some carcinogenic aromatic amines in four species of marine sponges. Comp Biochem Physiol. 86C:1986;17-22.
    • (1986) Comp Biochem Physiol , vol.86 , pp. 17-22
    • Kurelec, B.1    Britvic, S.2    Krca, S.3    Muller, W.E.G.4    Zahn, R.K.5
  • 31
    • 0013790728 scopus 로고
    • The osmotic adjustment in the euryhaline teleosts, the flounder, Pleuronectes flesus and the three-spined stickleback, Gasterosteus aculeatus
    • Lange R., Fugelli K. The osmotic adjustment in the euryhaline teleosts, the flounder, Pleuronectes flesus and the three-spined stickleback, Gasterosteus aculeatus. Comp Biochem Physiol. 15:1965;283-292.
    • (1965) Comp Biochem Physiol , vol.15 , pp. 283-292
    • Lange, R.1    Fugelli, K.2
  • 33
    • 0010444218 scopus 로고
    • The mixed function oxygenase system in molluscs: Metabolism, responses to xenobiotics and toxicity
    • Livingstone D.R., Arnold R., Chipman K., Kirchin M.A., Marsh J. The mixed function oxygenase system in molluscs: metabolism, responses to xenobiotics and toxicity. Oceanis. 16:1990;331-347.
    • (1990) Oceanis , vol.16 , pp. 331-347
    • Livingstone, D.R.1    Arnold, R.2    Chipman, K.3    Kirchin, M.A.4    Marsh, J.5
  • 34
    • 0026529659 scopus 로고
    • Activation of xenobiotics to reactive and mutagenic products by the marine invertebrates Mytilus edulis, Carcinus maenas and Asteria rubens
    • Marsh J.W., Chipman J.K., Livingstone D.R. Activation of xenobiotics to reactive and mutagenic products by the marine invertebrates Mytilus edulis, Carcinus maenas and Asteria rubens. Aquat Toxicol. 22:1992;115-128.
    • (1992) Aquat Toxicol , vol.22 , pp. 115-128
    • Marsh, J.W.1    Chipman, J.K.2    Livingstone, D.R.3
  • 35
    • 77956851720 scopus 로고
    • +ATPase and chloride cell function
    • In: Wood CM, Shuttleworth TJ, editors San Diego, CA: Academic Press
    • +ATPase and Chloride Cell Function. San Diego, CA: Academic Press, 1995:285-315.
    • (1995) +ATPase and Chloride Cell Function , pp. 285-315
    • McCormick, S.D.1
  • 36
    • 0025219875 scopus 로고
    • Myeloperoxidase catalyse cooxidative metabolism of methimazole: Oxidation of glutathione and NADH by free radical intermediates
    • McGirr L.G., Jatoe S.D., O'Brien P.J. Myeloperoxidase catalyse cooxidative metabolism of methimazole: oxidation of glutathione and NADH by free radical intermediates. Chem-Biol Interact. 73:1990;279-295.
    • (1990) Chem-Biol Interact , vol.73 , pp. 279-295
    • McGirr, L.G.1    Jatoe, S.D.2    O'Brien, P.J.3
  • 37
    • 0000106986 scopus 로고    scopus 로고
    • Biotransformation of xenobiotics
    • In: Klaassen CD, editor New York: McGraw-Hill
    • Parkinson A. Biotransformation of xenobiotics. In: Klaassen CD, editor. Biotransformation of Xenobiotics. New York: McGraw-Hill, 1996:113-186.
    • (1996) Biotransformation of Xenobiotics , pp. 113-186
    • Parkinson, A.1
  • 38
    • 0028961830 scopus 로고
    • Characterisation of hepatic flavin monooxygenase from the marine teleost, turbot (Scophthalmus maximus L.)
    • Peters L.D., Livingstone D.R., Shehin-Johnson S., Hines R.N., Schlenk D. Characterisation of hepatic flavin monooxygenase from the marine teleost, turbot (Scophthalmus maximus L.). Xenobiotica. 25:1995;121-131.
    • (1995) Xenobiotica , vol.25 , pp. 121-131
    • Peters, L.D.1    Livingstone, D.R.2    Shehin-Johnson, S.3    Hines, R.N.4    Schlenk, D.5
  • 39
    • 0018801101 scopus 로고
    • The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies
    • Poulsen L.L., Ziegler D.M. The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies. J Biol Chem. 254:1979;6449-6455.
    • (1979) J Biol Chem , vol.254 , pp. 6449-6455
    • Poulsen, L.L.1    Ziegler, D.M.2
  • 40
    • 0025826126 scopus 로고
    • Flavin-containing monooxygenase activity in liver microsomes form the rainbow trout Oncorhynchus mykiss
    • Schlenk D., Buhler D.R. Flavin-containing monooxygenase activity in liver microsomes form the rainbow trout Oncorhynchus mykiss. Aquat Toxicol. 20:1991;13-24.
    • (1991) Aquat Toxicol , vol.20 , pp. 13-24
    • Schlenk, D.1    Buhler, D.R.2
  • 41
    • 0025062491 scopus 로고
    • Flavin-containing monooxygenase activity in the gumboot chiton Cryptochiton stelleri
    • Schlenk D., Buhler D.R. Flavin-containing monooxygenase activity in the gumboot chiton Cryptochiton stelleri. Mar Biol. 104:1990;47-50.
    • (1990) Mar Biol , vol.104 , pp. 47-50
    • Schlenk, D.1    Buhler, D.R.2
  • 42
    • 0027415638 scopus 로고
    • Immunological characterization of flavin-containing monooxygenases from the liver of rainbow trout (Oncorhynchus mykiss): Sexual- And age-dependent differences and the effect of trimethylamine on enzyme regulation
    • Schlenk D., Buhler D.R. Immunological characterization of flavin-containing monooxygenases from the liver of rainbow trout (Oncorhynchus mykiss): sexual- and age-dependent differences and the effect of trimethylamine on enzyme regulation. Biochim Biophys Acta. 1156:1993;103-106.
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 103-106
    • Schlenk, D.1    Buhler, D.R.2
  • 43
    • 0026323408 scopus 로고
    • Role of flavin-containing monooxygenase in the in vitro biotransformation of aldicarb in rainbow trout (Oncorhynchus mykiss)
    • Schlenk D., Buhler D.R. Role of flavin-containing monooxygenase in the in vitro biotransformation of aldicarb in rainbow trout (Oncorhynchus mykiss). Xenobiotica. 21:1991;1583-1589.
    • (1991) Xenobiotica , vol.21 , pp. 1583-1589
    • Schlenk, D.1    Buhler, D.R.2
  • 44
    • 0025283613 scopus 로고
    • The in vitro biotransformation of 2-aminofluorene in the visceral mass of the Pacific oyster, Crassostrea gigas
    • Schlenk D., Buhler D.R. The in vitro biotransformation of 2-aminofluorene in the visceral mass of the Pacific oyster, Crassostrea gigas. Xenobiotica. 20:1990;563-572.
    • (1990) Xenobiotica , vol.20 , pp. 563-572
    • Schlenk, D.1    Buhler, D.R.2
  • 45
    • 0024938730 scopus 로고
    • Xenobiotic biotransformation in the Pacific oyster (Crassostrea gigas)
    • Schlenk D., Buhler D.R. Xenobiotic biotransformation in the Pacific oyster (Crassostrea gigas). Comp Biochem Physiol. 94C:1989;469-475.
    • (1989) Comp Biochem Physiol , vol.94 , pp. 469-475
    • Schlenk, D.1    Buhler, D.R.2
  • 46
    • 0027987512 scopus 로고
    • Characterization of liver flavin-containing monooxygenase of the smooth dogfish shark (Squalus acanthias) and partial purification of liver flavin-containing monooxygenase of the silky shark (Carcharhinus falciformis)
    • Schlenk D., Li-Schlenk R. Characterization of liver flavin-containing monooxygenase of the smooth dogfish shark (Squalus acanthias) and partial purification of liver flavin-containing monooxygenase of the silky shark (Carcharhinus falciformis). Comp Biochem Physiol. 109B:1994;655-664.
    • (1994) Comp Biochem Physiol , vol.109 , pp. 655-664
    • Schlenk, D.1    Li-Schlenk, R.2
  • 47
    • 0027200661 scopus 로고
    • A comparison of endogenous and exogenous substrates of the flavin-containing monooxygenases in aquatic organisms
    • Schlenk D. A comparison of endogenous and exogenous substrates of the flavin-containing monooxygenases in aquatic organisms. Aquat Toxicol. 26:1993;157-162.
    • (1993) Aquat Toxicol , vol.26 , pp. 157-162
    • Schlenk, D.1
  • 48
    • 0029437752 scopus 로고
    • Use of aquatic organisms as models to determine the in vivo contribution of flavin-containing monooxygenases to xenobiotic biotransformation
    • Schlenk D. Use of aquatic organisms as models to determine the in vivo contribution of flavin-containing monooxygenases to xenobiotic biotransformation. Mol Mar Biol Biotechnol. 4:1995;323-330.
    • (1995) Mol Mar Biol Biotechnol , vol.4 , pp. 323-330
    • Schlenk, D.1
  • 50
    • 77957182745 scopus 로고
    • The distribution, elimination, and in vivo biotransformation of aldicarb in the rainbow trout (Oncorhynchus mykiss)
    • Schlenk D., Erickson D.A., Lech J.J., Buhler D.R. The distribution, elimination, and in vivo biotransformation of aldicarb in the rainbow trout (Oncorhynchus mykiss). Fund Appl Toxicol. 18:1992;131-136.
    • (1992) Fund Appl Toxicol , vol.18 , pp. 131-136
    • Schlenk, D.1    Erickson, D.A.2    Lech, J.J.3    Buhler, D.R.4
  • 51
    • 0002050995 scopus 로고
    • Studies on myeloperoxidase activity in the common mussel, Mytilus edulis
    • Schlenk D., Martinez P.G., Livingstone D.R. Studies on myeloperoxidase activity in the common mussel, Mytilus edulis. Comp Biochem Physiol. 99C:1991;63-68.
    • (1991) Comp Biochem Physiol , vol.99 , pp. 63-68
    • Schlenk, D.1    Martinez, P.G.2    Livingstone, D.R.3
  • 52
    • 0030582261 scopus 로고    scopus 로고
    • Correlation of salinity with flavin-containing monooxygenase activity but not cytochrome P450 activity in the euryhaline fish (Platichthys flesus)
    • Schlenk D., Peters L.D., Livingstone D.R. Correlation of salinity with flavin-containing monooxygenase activity but not cytochrome P450 activity in the euryhaline fish (Platichthys flesus). Biochem Pharmacol. 52:1996;815-818.
    • (1996) Biochem Pharmacol , vol.52 , pp. 815-818
    • Schlenk, D.1    Peters, L.D.2    Livingstone, D.R.3
  • 53
    • 0029971142 scopus 로고    scopus 로고
    • Down-regulation of piscine flavin-containing monooxygenase by decreased salinity in euryhaline flounder (Platichthys flesus)
    • Schlenk D., Peters L.D., Livingstone D.R. Down-regulation of piscine flavin-containing monooxygenase by decreased salinity in euryhaline flounder (Platichthys flesus). Mar Environ Res. 42:1996;339-344.
    • (1996) Mar Environ Res , vol.42 , pp. 339-344
    • Schlenk, D.1    Peters, L.D.2    Livingstone, D.R.3
  • 54
    • 0029582973 scopus 로고
    • Differential expression and activity of flavin-containing monooxygenases in euryhaline and stenohaline flatfishes
    • Schlenk D., Peters L.D., Shehin-Johnson S., Hines R.N., Livingstone D.R. Differential expression and activity of flavin-containing monooxygenases in euryhaline and stenohaline flatfishes. Comp Biochem Physiol. 112C:1995;179-186.
    • (1995) Comp Biochem Physiol , vol.112 , pp. 179-186
    • Schlenk, D.1    Peters, L.D.2    Shehin-Johnson, S.3    Hines, R.N.4    Livingstone, D.R.5
  • 55
    • 0027434276 scopus 로고
    • Channel catfish liver monooxygenases. Immunological characterization of constitutive cytochromes P450 and the absence of active flavin-containing monooxygenases
    • Schlenk D., Ronis M.J., Miranda C.L., Buhler D.R. Channel catfish liver monooxygenases. Immunological characterization of constitutive cytochromes P450 and the absence of active flavin-containing monooxygenases. Biochem Pharmacol. 45:1993;217-221.
    • (1993) Biochem Pharmacol , vol.45 , pp. 217-221
    • Schlenk, D.1    Ronis, M.J.2    Miranda, C.L.3    Buhler, D.R.4
  • 56
    • 0029833323 scopus 로고    scopus 로고
    • Identification of tissue-specific DNAse I hypersensitive sites in the rabbit flavin-containing monooxygenase form 2 (FMO2) gene
    • Shehin-Johnson S.E., Hines R.N. Identification of tissue-specific DNAse I hypersensitive sites in the rabbit flavin-containing monooxygenase form 2 (FMO2) gene. Drug Metab Dispos. 24:1996;891-898.
    • (1996) Drug Metab Dispos , vol.24 , pp. 891-898
    • Shehin-Johnson, S.E.1    Hines, R.N.2
  • 59
    • 0000776566 scopus 로고
    • Biosynthesis of trimethylamine oxide in Calanus finmarchicus, properties of a soluble trimethylamine monooxygenase
    • Strom A.R. Biosynthesis of trimethylamine oxide in Calanus finmarchicus, properties of a soluble trimethylamine monooxygenase. Comp Biochem Physiol. 65B:1980;243-249.
    • (1980) Comp Biochem Physiol , vol.65 , pp. 243-249
    • Strom, A.R.1
  • 60
    • 0001975051 scopus 로고
    • Biochemistry of non-protein nitrogenous compounds in fish including the use of amino acids for anaerobic energy production
    • Van Waarde A. Biochemistry of non-protein nitrogenous compounds in fish including the use of amino acids for anaerobic energy production. Comp Biochem Physiol. 91B:1988;207-228.
    • (1988) Comp Biochem Physiol , vol.91 , pp. 207-228
    • Van Waarde, A.1
  • 62
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanisms and substrate specificities
    • Ziegler D.M. Flavin-containing monooxygenases: catalytic mechanisms and substrate specificities. Drug Metab Rev. 19:1988;1-32.
    • (1988) Drug Metab Rev , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 63
    • 0027462628 scopus 로고
    • Recent studies on the structure and function of multisubstrate flavin-containing monooxygenases
    • Ziegler D.M. Recent studies on the structure and function of multisubstrate flavin-containing monooxygenases. Ann Rev Pharmacol Toxicol. 33:1993;179-199.
    • (1993) Ann Rev Pharmacol Toxicol , vol.33 , pp. 179-199
    • Ziegler, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.