The binding affinity of carcinogenic N-nitrosodimethylamine and N-nitrosomethylaniline to cytochromes P450 2B4, 2E1 and 3A6 does not dictate the rate of their enzymatic N- demethylation.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F10%3A10069745" target="_blank" >RIV/00216208:11310/10:10069745 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/10:00434973
Result on the web
—
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
The binding affinity of carcinogenic N-nitrosodimethylamine and N-nitrosomethylaniline to cytochromes P450 2B4, 2E1 and 3A6 does not dictate the rate of their enzymatic N- demethylation.
Original language description
The interaction of carcinogenic N-nitrosodimethylamine (NDMA) and N-nitrosomethylaniline (NMA) with cytochromes P450 (CYP), CYP2B4, CYP2E1 and CYP3A6, and their metabolism by these enzymes reconstituted with NADPH-CYP reductase in liposomes were studiedin this work.
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
<a href="/en/project/GA303%2F09%2F0472" target="_blank" >GA303/09/0472: Study on participation of biotransformation enzymes in development of renal injury and urothelial cancer mediated by aristolochic acid</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>R - Projekt Ramcoveho programu EK
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
General Physiology and Biophysics
ISSN
0231-5882
e-ISSN
—
Volume of the periodical
29
Issue of the periodical within the volume
2
Country of publishing house
SK - SLOVAKIA
Number of pages
11
Pages from-to
—
UT code for WoS article
000279094900008
EID of the result in the Scopus database
—