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1 In vitro and in vivo inhibition of human flavin-containing monooxygenase form 3 (FMO3) in the presence of dietary indoles
article 1999    
Author: Cashman, J.R. · Xiong, Y. · Lin, J. · Verhagen, H. · Poppel, G. van · Bladeren, P.J. van · Larsen-Su, S. · Williams, D.E.
Keywords: Nutrition · Dietary indoles · Human flavin-containing monooxygenase · Indole-3-carbinol-related inhibitors · Trimethylamine N-oxygenation inhibitors · 3 indolemethanol · Complementary DNA · Flavin containing monooxygenase 3 · Glucosinolate · Hydrochloric acid · Indole derivative · Isoenzyme · Trimethylamine · Trimethylamine oxide · Unclassified drug · Unspecific monooxygenase · Adult · Controlled study · Dietary intake · Enzyme activity · Enzyme inhibition · Gas chromatography · Gastrointestinal tract · High performance liquid chromatography · Human · Human experiment · Male · Mass spectrometry · Normal human · Oral drug administration · Polymerization · Priority journal · Volunteer · Xenobiotic metabolism · Adult · Antioxidants · Brassica · Carrier Proteins · Cross-Over Studies · Diet · Humans · Indoles · Male · Methylamines · Oxygenases
[Abstract]

2 Purification and characterization of a Baeyer-Villiger mono-oxygenase from Rhodococcus erythropolis DCL14 involved in three different monocyclic monoterpene degradation pathways
article 2000    
Author: Werf, M.J. van der
Keywords: Nutrition · Carvone · Flavoprotein · Limonene · Menthol · Regioselectivity · Bacterial enzyme · Carvone · Cyclohexanone derivative · Heptanoic acid derivative · Limonene · Menthone · Terpene · Unspecific monooxygenase · Amino acid sequence · Amino terminal sequence · Biodegradation · Enzyme activity · Enzyme analysis · Enzyme purification · Enzyme specificity · Enzyme structure · Molecular weight · Nonhuman · Priority journal · Rhodococcus · Sequence homology · Stereochemistry · Aldehydes · Amino Acid Sequence · Biodegradation, Environmental · Catalysis · Cyclohexanones · Enzyme Induction · Enzyme Inhibitors · Flavin-Adenine Dinucleotide · Hydrogen-Ion Concentration · Menthol · Metals · Molecular Sequence Data · Molecular Weight · Oxygenases · Rhodococcus · Sequence Alignment · Sequence Homology, Amino Acid · Spectrum Analysis · Stereoisomerism · Substrate Specificity · Temperature · Terpenes
[Abstract]

3 Inhibition of tolbutamide 4-methylhydroxylation by a series of non-steroidal anti-inflammatory drugs in V79-NH cells expressing human cytochrome P4502C10
article 1996    
Author: Kappers, W.A. · Groene, E.M. de · Kleij, L.A. · Witkamp, R.F. · Zweers-Zeilmaker, W.M. · Feron, V.J. · Horbach, G.J.
Keywords: Toxicology · CYP2C9 protein, human · cytochrome P450 · diclofenac · enzyme inhibitor · flurbiprofen · ketoprofen · mixed function oxidase · nonsteroid antiinflammatory agent · phenylbutazone · sulfaphenazole · tolbutamide · tolbutamide 4 hydroxylase · tolbutamide 4-hydroxylase · unspecific monooxygenase · animal · article · cell line · Cricetulus · drug interaction · gene expression · genetic transfection · genetics · hamster · human · hydroxylation · lung · metabolism · methylation · Animals · Anti-Inflammatory Agents, Non-Steroidal · Aryl Hydrocarbon Hydroxylases · Cell Line · Cricetinae · Cricetulus · Cytochrome P-450 Enzyme System · Diclofenac · Drug Interactions · Enzyme Inhibitors · Flurbiprofen · Gene Expression · Humans · Hydroxylation · Ketoprofen · Lung · Methylation · Mixed Function Oxygenases · Phenylbutazone · Sulfaphenazole · Tolbutamide · Transfection
[Abstract]

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