Nicotine C-oxidation by human liver microsomes
Read Online
Share

Nicotine C-oxidation by human liver microsomes a major role for CYP2A6.

  • 151 Want to read
  • ·
  • 52 Currently reading

Published by National Library of Canada in Ottawa .
Written in English


Book details:

Edition Notes

Thesis (M.Sc.) -- University of Toronto, 1996.

SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL16973815M
ISBN 10061219213X
OCLC/WorldCa46562417

Download Nicotine C-oxidation by human liver microsomes

PDF EPUB FB2 MOBI RTF

A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes. Messina ES(1), Tyndale RF, Sellers EM. Author information: (1)The Addiction Research Foundation and the Department of Pharmacology, University of Toronto, Ontario, Canada. Nicotine is primarily metabolized to cotinine by cytochromes P Cited by: Messina ES, Tyndale RF, Sellers EM () A major role for CYP2A6 in nicotine C-oxidation by human liver microsomes. J Pharmacol Exp Ther (3)– PubMed Google Scholar Meunier V, Bourrie M, Julian B, Marti E, Guillou F, Berger Y, Fabre G () Expression and induction of CYP1A1/1A2, CYP2A6 and CYP3A4 in primary cultures of human Cited by: N-Oxygenation of Primary Amines and Hydroxylamines and Retroreduction of Hydroxylamines by Adult Human Liver Microsomes and Adult Human Flavin-Containing Monooxygenase 3. Chemical Cited by:   In the presence of human brain microsomes, along with nicotine‐ N ‐oxidation, we also detect nicotine oxidation to nicotine iminium ion. However, unlike N ‐oxidation, this activity is NADPH independent, does not follow Michaelis‐Menten kinetics, and is not inhibited by NADP or carbon by: 2.

Request PDF | Nicotinamide N-Oxidation by CYP2E1 in Human Liver Microsomes | Excess nicotinamide, a form of vitamin B(3), is metabolized through two enzymatic systems and eventually . In the presence of human brain microsomes, along with nicotine‐N‐oxidation, we also detect nicotine oxidation to nicotine iminium ion. However, unlike N‐oxidation, this activity is NADPH. Nicotine & Tobacco Research , DOI: /ntr/ntr Mitsuo Miyazawa, Shinsuke Marumoto, Toshiyuki Takahashi, Hiroshi Nakahashi, Risa Haigou, Kyousuke Nakanishi. Metabolism of (+)- and (-)-Menthols by CYP2A6 in Human Liver by: In vitro studies using human liver microsomes revealed that the menthol enantiomers, (+)-menthol and (À)-menthol, are oxidised in the liver principally by the CYP2A6 enzyme to (+)-trans-p.

  However, nicotine and cotinine are both glucuronidated at the nitrogen atom of the pyridine ring. We report here that human liver microsomes catalyze both the N-glucuronidation and the O-glucuronidation of trans-3‘ Cited by: by nicotine, cotinine, and an aqueous cigarette tar extract (ACTE) in human 2E1-expressing microsomes. At all substrate concentrations (0– mM) nicotine was a significantly more potent inhibitor of CYP 2E1 activity compared to cotinine. Estimated Ki values for nicotine . Nicotine or cotinine was incubated with human liver microsomes and UDP-glucuronic acid in a μl incubation mixture. The nicotine N -glucuronide (Nic-glu) and cotinine N -glucuronide (Cot-glu) formed were analyzed by ion-pair chromatography with a C Cited by: 8. The formation of both cis- and trans-nicotine-1'-N-oxide in rat liver microsomes was inhibited by the addition of 1-(1-naphthyl)thiourea or by heat-treatment of microsomes. 2-Diethylaminoethyl.