Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
DOI
PMC
 |
|
Open Access Green as soon as Postprint is submitted to ZB.
Human liver debrisoquine 4-hydroxylase: Test for specifity toward various monooxygenase substrates and model of the active site.
Arch. Toxicol. 60, 89-90 (1987)
Polyclonal antibodies raised toward a debrisoquine 4-hydroxylating cytochrome P-450 species purified from rat liver (P-450UTA) were used to determine which monooxygenase reactions are linked to debrisoquine hydroxylation in human liver. Anti P-450UTA did not inhibit the oxidation of dimethylnitrosamine, morphine, diazepam, vinylidene chloride, trichloroethylene, benzo(a)pyrene and its 7.8-dihydrodiol, but was inhibitory for the hydroxylation of debrisoquine, (±)-bufuralol, lasiocarpine and monocrotaline. A model interpreting the substrate specificity of the human liver enzyme is presented. .
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cytochrome P-450 ; Debrisoquine ; Human Liver
ISSN (print) / ISBN
0340-5761
e-ISSN
1432-0738
Journal
Archives of Toxicology
Quellenangaben
Volume: 60,
Issue: 1-3,
Pages: 89-90
Publisher
Springer
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institut für Toxikologie und Biochemie