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Xenobiotica
the fate of foreign compounds in biological systems
Volume 18, 1988 - Issue 1
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Research Article

Inhibition of nasal and liver cytochrome P-450 mono-oxygenases by dioxolanes

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Pages 1-9 | Received 07 May 1986, Published online: 22 Sep 2008

References

  • Böhlen P., Stein S., Dairman W., Udenfriend S. Fluorometric assay of proteins in the nanogram range. Archives of Biochemistry and Biophysics 1973; 155: 213–220
  • Burke M. D., Prough A. R., Mayer R. T. Characteristics of a microsomal cytochrome P-448-mediated reaction ethoxyresorufin O-de-ethylation. Drug Metabolism and Disposition 1977; 5: 1–8
  • Dahl A. R., Brezinski A. D. Inhibition of rabbit nasal and hepatic cytochrome P-450-dependent hexamethylphosphoramide (HMPA) N-demethylase by methylenedioxyphenyl compounds. Biochemical Pharmacology 1985; 34: 631–636
  • Dahl A. R., Hadley M. W. Cytochrome P-450-dependent monooxygenase activity in nasal membranes of six species. Drug Metabolism and Disposition 1983; 11: 275–276
  • Dahl A. R., Hall L., Hadley W. M. Characterization and partial purification of rabbit nasal cytochrome P-450. Toxicologist 1983; 3: 91
  • Dahl A. R., Hodgson E. Interactions of heme enzymes with π-acceptor ligands. Federation Proceedings of the Federation of American Societies of Experimental Biology 1976; 35: 379
  • Dahl A. R., Hodgson E. The interaction of aliphatic analogs of methylenedioxpheyl compounds with cytochromes P-450 and P-420. Chemico-Biological Interactions 1979; 27: 163–175
  • Ding X., Koop D. R., Coon M. J. Extrahepatic identification of ethanol-enducible rabbit cytochrome P-450 isozyme 3a. Federation Proceedings of the Federation of American Societies of Experimental Biology 1985; 44: 1449
  • Hansch C., Leo J. A. Substituent Constants for Correlation Analysis in Chemistry and Biology. Wiley and Sons, New York 1979; 48
  • Hodgson E., Philpot R. M. Interaction of methylenedioxyphenyl ‘1,3-benzodioxole’ compounds with enzymes and their effects on mammals. Drug Metabolism Reviews 1974; 3: 231–301
  • Miyake Y., Gaylor J. L., Morris H. P. Abnormal microsomal cytochromes and electron transport in Morris hepatomas. Journal of Biological Chemistry 1974; 249: 1980–1987
  • Murray M., Hetnarski K., Wilkinson C. F. Selective inhibitory interactions of alkoxymethylenedioxybenzenes towards mono-oxygenase activity in rat-hepatic microsomes. Xenobiotica 1985a; 15: 369–379
  • Murray M., Marcus C. B., Wilkinson C. F. Quantitative structure-activity relationships in the displacement of the dihydrosafrole metabolite-cytochrome P-450 complex. Quantitative Structure-Activity Relationship. 1985b; 4: 18–22
  • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. Journal of Biological Chemistry 1964a; 239: 2370–2378
  • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. Journal of Biological Chemistry 1946b; 239: 2379–2385
  • Ullrich V., Nastainszyk W., Ruf H. Ligand reactions of cytochrome-P-450. Biochemical Society Transactions 1975; 3: 803–807
  • Wilkinson C. F., Murray M., Marcus C. B. Interactions of methylenedioxy-phenyl compounds with cytochrome P-450 and effects on microsomal oxidation. Reviews in Biochemical Toxicology, E. Hodgson, J. R. Bend, R. M. Philpot. Elsevier Science Publishing Company, Inc., New York 1984; Vol. 6: 27–63

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