نتایج جستجو برای: cytochrome p 450 inhibition

تعداد نتایج: 1607174  

Journal: :The Biochemical journal 1992
J S Miles A W Munro B N Rospendowski W E Smith J McKnight A J Thomson

1. The gene CYP102 encoding cytochrome P-450 BM-3 and subgenes encoding the cytochrome P-450 and cytochrome P-450 reductase domains have been cloned in Escherichia coli. 2. The protein products of these genes have been overexpressed and purified to homogeneity. 3. The cytochrome P-450 domain is purified in the ferric low-spin state, but is readily converted into the high-spin state by addition ...

Journal: :Molecular pharmacology 2013
Clinton R Nishida Steven Everett Paul R Ortiz de Montellano

Cytochrome P450 (P450)-catalyzed oxidation of the aromatic ring of estradiol can result in 2- or 4-hydroxylation. Which of these products is formed is biologically important, as the 4-hydroxylated metabolite is carcinogenic, whereas the 2-hydroxylated metabolite is not. Most human P450 enzymes, including CYP1A1 and CYP1A2, exhibit a high preference for estradiol 2-hydroxylation, but human CYP1B...

2012
Beihua Bao Ting Geng Yudan Cao Weifeng Yao Li Zhang Anwei Ding

The aim of this study was to find out whether Schizonepetin influences the pharmacokinetics of the main substrates drugs of CYP1A2, CYP3A1/2, CYP2E1, CYP2C19 and CYP2D6 in rats; the influence on the levels of CYP mRNA was also studied. Phenacetin, dapsone, chlorzoxazone, omeprazole and metoprolol were selected as probe substrates for CYP1A2, CYP3A1/2, CYP2E1, CYP2C19 and CYP2D6 respectively. HP...

Journal: :The Biochemical journal 2012
James R Reed J Patrick Connick Dongmei Cheng George F Cawley Wayne L Backes

Previous studies have shown that the presence of one P450 enzyme can affect the function of another. The goal of the present study was to determine if P450 enzymes are capable of forming homomeric complexes that affect P450 function. To address this problem, the catalytic activities of several P450s were examined in reconstituted systems containing NADPH-POR (cytochrome P450 reductase) and a si...

Journal: :Comparative biochemistry and physiology. Toxicology & pharmacology : CBP 2003
Shin-Pei Yang Theresa Medling Gregory M Raner

Xenobiotic metabolism in the tongue has received little attention in the literature. In the present study, we report a comparative analysis of constitutive cytochrome P450 (CYP) expression and activities in the tongue. First we compared catalytic activities of rabbit, rat and bovine tongue samples using the probe substrates 4-nitrophenol, 1-phenylethanol, caffeine and 7-ethoxycoumarin. Rabbit t...

Journal: :Plant physiology 1991
B A Halkier B L Møller

The biosynthesis of the tyrosine-derived cyanogenic glucoside dhurrin involves N-hydroxytyrosine, (E)- and (Z)-p-hydroxyphenylacetaldehyde oxime, p-hydroxyphenylacetonitrile, and p-hydroxymandelonitrile as intermediates and has been studied in vitro using a microsomal enzyme system obtained from etiolated sorghum (Sorghum bicolor [L.] Moench) seedlings. The biosynthesis is inhibited by carbon m...

2003
ATTALLAH KAPPAS

Liver microsomes contain a mixed function oxidase system capable of metabolizing a broad range of biologically active substances, including drugs, steroids, and environmental chemicals such as polycyclic hydrocarbons. Certain hemoproteins, collectively referred to as cytochrome P-450, function as the terminal oxidase in this system. The fact that this hepatic mixed function oxidase system is se...

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