Title : N-nitroso compounds induce changes in carcinogen-metabolizing enzymes.

Pub. Date : 1996 Sep 10

PMID : 8844979






4 Functional Relationships(s)
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1 The bioactivation of N-nitrosoamines and polycyclic aromatic hydrocarbons (PAH) is mediated by the mixed function oxidase system, which includes dimethylnitrosamine N-demethylase I (DMN-dI), arylhydrocarbon hydroxylase (AHH), cytochrome P-450, cytochrome b5 and NADPH-cytochrome c reductase of liver microsomes. Polycyclic Aromatic Hydrocarbons cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus
2 The bioactivation of N-nitrosoamines and polycyclic aromatic hydrocarbons (PAH) is mediated by the mixed function oxidase system, which includes dimethylnitrosamine N-demethylase I (DMN-dI), arylhydrocarbon hydroxylase (AHH), cytochrome P-450, cytochrome b5 and NADPH-cytochrome c reductase of liver microsomes. Polycyclic Aromatic Hydrocarbons cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus
3 The bioactivation of N-nitrosoamines and polycyclic aromatic hydrocarbons (PAH) is mediated by the mixed function oxidase system, which includes dimethylnitrosamine N-demethylase I (DMN-dI), arylhydrocarbon hydroxylase (AHH), cytochrome P-450, cytochrome b5 and NADPH-cytochrome c reductase of liver microsomes. Polycyclic Aromatic Hydrocarbons cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus
4 The bioactivation of N-nitrosoamines and polycyclic aromatic hydrocarbons (PAH) is mediated by the mixed function oxidase system, which includes dimethylnitrosamine N-demethylase I (DMN-dI), arylhydrocarbon hydroxylase (AHH), cytochrome P-450, cytochrome b5 and NADPH-cytochrome c reductase of liver microsomes. Polycyclic Aromatic Hydrocarbons cytochrome P450, family 1, subfamily a, polypeptide 1 Mus musculus