Characterization of hepatic flavin monooxygenase from the marine teleost turbot (Scophthalmus maximus L.)

References

• Ágústsson I., Strøm A. R. Biosynthesis and turnover of trimethylamine oxide in the teleost cod. Gadus morhua. Journal of Biological Chemistry 1981; 256: 8045–8049
   PubMedGoogle Scholar
• Charest R. P., Chenoweth M., Dunn A. Metabolism of trimethylamines in kelp bass (Paralabrax clathratus) and marine and freshwater pink salmon (Oncorhynchus gorbuscha). Journal of Comparative Physiology B 1988; 158: 609–619
   PubMedGoogle Scholar
• Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry 1987; 162: 156–159
   PubMed Web of Science ®Google Scholar
• Daikoku T., Murata M., Sakaguchi M. Effects of intraperitoneally injected and dietary trimethylamine on the biosynthesis of trimethylamine oxide in relation to sea water adaption of the eel, Anguilla japonica and the guppy. Poecilia reticulata. Comparative Biochemistry and Physiology 1988; 89A: 261–264
   Google Scholar
• Dannan G. A., Guengerich F. P., Waxman D. J. Hormonal regulation of rat liver microsomal enzymes. Role of gonadal steroids in programming, maintenance and suppression of β 4-steroid 5 α reductase, flavin-containing monooxygenase and sex specific cytochromes P450. Journal of Biological Chemistry 1986; 261: 10728–10735
   PubMed Web of Science ®Google Scholar
• Duffel M. W., Graham J. M., Ziegler D. M. Changes in dimethylaniline N-oxidase activity of mouse liver and kidney induced by steroid sex hormones. Molecular Pharmacology 1981; 19: 134–139
   PubMed Web of Science ®Google Scholar
• Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Annals of Biochemistry 1983; 132: 6–13
   Web of Science ®Google Scholar
• Feinberg A. P., Vogelstein B. Appendum: A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Annals of Biochemistry 1984; 137: 226–267
   Google Scholar
• Goldstein L., Dewitt-Harley S. Trimethylamine oxidase of nurse shark liver and its relation to mammalian mixed function amine oxidase. Comparative Biochemistry and Physiology 1973; 45B: 895–903
   Google Scholar
• 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. Toxicology and Applied Pharmacology 1994; 125: 1–6
   PubMed Web of Science ®Google Scholar
• Houdi A. A., Damani L. A. N-demethylation and N-oxidation of N,N-dimethylaniline by rat liver microsomes. Biological Oxidation of Nitrogen in Organic Molecules, J. W. Gorrod, L. A. Damani. Ellis Horwood, Chichester 1985; 96–100
   Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Lawton M. P., Gasser R., Tynes R. E., Hodgson E., Philpot R. M. The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes. Journal of Biological Chemistry 1990; 256: 5855–5861
   Google Scholar
• Livingstone D. R. Organic xenobiotic metabolism in marine invertebrates. Comparative and Environmental Physiology, R. Gilles. Springer, Berlin 1991; vol. 7: 45–185
   Google Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the folin reagent. Journal of Biological Chemistry 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Pang P. K. T., Griffith R. W., Atz J. W. Osmoregulation in elasmobranchs. American Zoologist 1977; 17: 365–377
   Google Scholar
• Schlenk D. Xenobiotic biotransformation in aquatic organisms. Oregon State University. 1989, Doctoral dissertation
   Google Scholar
• Schlenk D. A comparison of endogenous and exogenous substrates of the flavin-containing monooxygenases in aquatic organisms. Aquatic Toxicology 1993; 26: 157–163
   Google Scholar
• Schlenk D., Buhler D. R. Xenobiotic biotransformation in the pacific oyster (Crassostrea gigas). Comparative Biochemistry and Physiology 1989; 94C: 469–475
   Google Scholar
• Schlenk D., Buhler D. R. Role of flavin-containing monooxygenase in the in vitro biotransformation of aldicarb in rainbow trout (Oncorhynchus mykiss). Xenobiotica 1991a; 21: 1583–1589
   PubMed Web of Science ®Google Scholar
• Schlenk D., Buhler D. R. Flavin-containing monooxygenase activity in liver microsomes from the rainbow trout (Oncorhynchus mykiss). Aquatic Toxicology 1991b; 20: 13–24
   Web of Science ®Google Scholar
• Schlenk D., Buhler D. R. Immunological characterization of flavin-containing monooxy-genase in the liver of rainbow trout, Oncorhynchus mykiss: studies on the sex- and age-dependent differences and the effect of trimethylamine on enzyme regulation. Biochimica et Biophysica Acta 1993; 1156: 103–106
   PubMedGoogle Scholar
• Schlenk D., Li-Schlenk R. Characterization of liver flavin-containing monooxygenase of the smooth dogfish shark (Squalas acanthus) and partial purification of liver flavin-containing monooxygenase of the silky shark (Carcharhinus falciformis). Comparative Biochemistry and Physiology 1995, in press
   Google Scholar
• Stegeman J. J., Hahn M. Biochemistry and molecular biology of monooxygenases: current perspectives on forms, functions and regulation of cytochrome P450 in aquatic species. Aquatic Toxicology: Molecular, Biochemical and Cellular Perspectives, D. Malins, G. Ostrander. Lewis, Boca Raton 1994; 87–206
   Google Scholar
• Strøm A. R. Biosynthesis of trimethylamine oxide in Calanus finmarchicus. Properties of a soluble trimethylamine monooxygenase. Comparative Biochemistry and Physiology 1980; 65B: 243–249
   Google Scholar
• Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences USA 1979; 76: 4350–4354
   PubMed Web of Science ®Google Scholar
• Varanasi U., Stein J. E., Nishimoto M. Biotransformation and disposition of PAH in fish. Metabolism of Polycyclic Aromatic Hydrocarbons in the Aquatic Environment, U. Varanasi. CRC Press, Boca Raton 1989; 93–149
   Google Scholar
• Persistent Pollutants in Marine Ecosystems, C. H. Walker, D. R. Livingstone. Pergamon, Oxford 1992
   Google Scholar
• Williams D. E., Hale S. E., Muerhoff A. S., Masters B. S. S. Rabbit lung FMO: purification, characterization and induction during pregnancy. Biochemical Pharmacology 1985; 30: 381–390
   Google Scholar
• Ziegler D. M. Flavin-containing monooxygenases: catalytic mechanisms and substrate specificities. Drug Metabolism Review 1988; 19: 1–32
   PubMed Web of Science ®Google Scholar
• Ziegler D. M. Recent studies on the structure and function of multisubstrate flavin-containing monooxygenases. Annual Review of Pharmacology and Toxicology 1993; 33: 179–199
   PubMed Web of Science ®Google Scholar
• Ziegler D. M., Mitchell C. H. Microsomal oxidase. IV. Properties of a mixed function amine oxidase isolated from pig liver microsomes. Archives of Biochemistry and Biophysics 1972; 150: 116–125
   PubMed Web of Science ®Google Scholar
• Ziegler D. M., Pettit F. H. Formation of an intermediate N-oxide in the oxidative demethylation of N,N-dimethylaniline catalysed by liver microsomes. Biochemistry and Biophysics Research Communications 1964; 15: 188–193
   PubMed Web of Science ®Google Scholar