Denitrosation of N-nitrosomorpholine by liver microsomes; possible role of cytochrome P-450. 1980

K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz

Liver microsomes from male mice and rats were incubated with N-nitrosomorpholine (MoNA) and an NADPH-regenerating system. The formation of nitrite was measured after induction or inhibition of the microsomal monooxygenase system. Pretreatment of the animals with phenobarbital (PB) enhanced nitrite formation by about 200%, while 3-methylcholanthrene (3-MC)-induction showed no exceptional effects. Various specific inhibitors of the monooxygenase function including carbon monoxide decreased nitrite formation. In conjunction with results obtained by spectra studies it is suggested that N-nitrosomorpholine is denitrosated by a reduction process in which cytochrome (cyt.) P-450 seems to be involved. Nitricoxide formed is partly converted to nitrite under these conditions.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008297 Male Males
D008658 Inactivation, Metabolic Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion. Detoxication, Drug, Metabolic,Drug Detoxication, Metabolic,Metabolic Detoxication, Drug,Detoxification, Drug, Metabolic,Metabolic Detoxification, Drug,Metabolic Drug Inactivation,Detoxication, Drug Metabolic,Detoxication, Metabolic Drug,Detoxification, Drug Metabolic,Drug Inactivation, Metabolic,Drug Metabolic Detoxication,Drug Metabolic Detoxification,Inactivation, Metabolic Drug,Metabolic Drug Detoxication,Metabolic Inactivation
D008748 Methylcholanthrene A carcinogen that is often used in experimental cancer studies. 20-Methylcholanthrene,3-Methylcholanthrene,20 Methylcholanthrene,3 Methylcholanthrene
D008862 Microsomes, Liver Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough. Liver Microsomes,Liver Microsome,Microsome, Liver
D009025 Morpholines Tetrahydro-1,4-Oxazines,Tetrahydro 1,4 Oxazines
D009573 Nitrites Salts of nitrous acid or compounds containing the group NO2-. The inorganic nitrites of the type MNO2 (where M Nitrite
D009602 Nitrosamines A class of compounds that contain a -NH2 and a -NO radical. Many members of this group have carcinogenic and mutagenic properties. Nitrosamine
D010634 Phenobarbital A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations. Phenemal,Phenobarbitone,Phenylbarbital,Gardenal,Hysteps,Luminal,Phenobarbital Sodium,Phenobarbital, Monosodium Salt,Phenylethylbarbituric Acid,Acid, Phenylethylbarbituric,Monosodium Salt Phenobarbital,Sodium, Phenobarbital
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450

Related Publications

K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
January 1981, Advances in experimental medicine and biology,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
June 1972, La Nouvelle presse medicale,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
November 1968, Molecular pharmacology,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
October 1985, Archives of biochemistry and biophysics,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
May 1993, Pharmacology,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
August 1971, Chemico-biological interactions,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
August 1989, Biulleten' eksperimental'noi biologii i meditsiny,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
January 1976, Farmakologiia i toksikologiia,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
June 1982, Archives of biochemistry and biophysics,
K E Appel, and D Schrenk, and M Schwarz, and B Mahr, and W Kunz
December 1986, European journal of biochemistry,
Copied contents to your clipboard!