Interactions of heterocyclic Maillard products with the hepatic microsomal monooxygenase system
| Autor: | Wolfgang Legrum, G. Koss, B. Hahnemann, Karl J. Netter |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Male
Cytochrome Stereochemistry Health Toxicology and Mutagenesis Metabolite 7-Alkoxycoumarin O-Dealkylase Toxicology Biochemistry Mixed Function Oxygenases Mice symbols.namesake chemistry.chemical_compound Cytochrome P-450 Enzyme System Biotransformation Animals Pharmacology biology Spectrum Analysis Cytochrome P450 General Medicine Metabolism Maillard Reaction Flavoring Agents Maillard reaction chemistry Microsomes Liver biology.protein Microsome symbols |
| Zdroj: | Xenobiotica. 19:1319-1326 |
| ISSN: | 1366-5928 0049-8254 |
| DOI: | 10.3109/00498258909043183 |
| Popis: | 1. Interactions of methyl-substituted pyrazines, and other constituents of Maillard products generated during heat treatment of food, with hepatic microsomal mixed-function oxygenases were studied in vitro. 2. Spectral interactions of N-containing heteroaromatic compounds with the cytochrome P-450 system are type I or type II depending on the state of induction, and are relatively weak. Inhibition of 7-ethoxycoumarin O-deethylation by these compounds is ten times lower than that of metyrapone, agreeing with the weak spectral interaction. Inhibition is competitive for 2,3-dimethylquinoxaline, and complex for 2,5-dimethylpyrazine and 2,3,5,6-tetramethylpyrazine. 3. Spectral and inhibitory interactions indicate biotransformation. This was studied with 2,3,5,6-tetramethylpyrazine; the metabolite formed was identified as 2-hydroxymethyl-3,5,6-trimethylpyrazine. Metabolism to the N-oxide did not occur. |
| Databáze: | OpenAIRE |
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