Results 1 to 10 of about 778,835 (257)
Role of phospholipid in electron transfer in a reconstituted liver microsomal enzyme system containing cytochrome P-450 [PDF]
Chemico-Biological Interactions, 1971 Abstract Phosphatidylcholine, which is required for fatty acid, hydrocarbon and drug hydroxylation in a reconstituted liver microsomal enzyme system, is essential for the enzymatic reduction of cytochrome P-450.
Minor J. Coon +2 more
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Phospholipid requirement for dimethylnitrosamine demethylation by hamster hepatic microsomal cytochrome P-450 enzyme system [PDF]
Biochemical Journal, 1976 Extraction with butan-1-ol of freeze-dried microsomal fractions from livers of 3-methyl-cholarthrene-pre-treated hamsters removed about 90% of the total lipid content, but the lipid remaining proved sufficient for the cytochrome P-450 enzyme system to retain about 15-40% of its original catalytic activity for dimethylnitrosamine demethylation. Addition
Prabhakar D. Lotlikar +3 more
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Enzyme Activity of the Cytochrome P-450 Monooxygenase System in the Presence of Single Chain Lipid Molecules [PDF]
Zeitschrift für Naturforschung C, 2001 Abstract The influence of single chain lipids on the 7-ethoxycoumarin O-deethyase activity of the reconstituted binary protein complex of isolated cytochrome P450 and NADPH-cytochrome P450 reductase has been examined. The enzyme activity of this binary enzyme complex has been shown to be influenced by (i) altering the complexation ...
Dieter Müller‐Enoch +3 more
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Inhibitory Effects of Pteridines on the Cytochrome P-450 Enzyme System [PDF]
Pteridines, 1997 The effects of 17 different pteridine derivatives on rat liver microsomal cytochrome P-450 catalyzed degradation of aminoantipyrin were studied. Neopterin (41% of control), biopterin (42%), monapterin (73%), pterin (74%), lumazine (75%) and 6-methylpterin (77%) significantly inhibit the degradation of aminoantipyrin.
Renate Horejsi +5 more
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Properties of a Yeast Cytochrome P‐450‐Containing Enzyme System which Catalyzes the Hydroxylation of Fatty Acids, Alkanes, and Drugs [PDF]
European Journal of Biochemistry, 1973 The growth of Candida tropicalis on tetradecane causes the induction of a cytochrome P‐450‐containing enzyme system which catalyzes the hydroxylation of fatty acids, hydrocarbons and drugs. When the cells are broken by treatment with a French pressure cell, the cytochrome P‐450 is obtained in an apparently soluble form.
Wilfried Duppel +2 more
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Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system [PDF]
Biochemical Journal, 1975 Oxidative demethylation of dimethylnitosamine was studied with both reconstituted and unresolved liver microsomal cytochrome P-450 enzyme systems from rats and hamsters. Proteinase treatment of liver microsomal preparations yielded cytochrome P-450 particulate fractions.
Prabhakar D. Lotlikar +2 more
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Ontogeny of the chicken cytochrome P-450 enzyme system
Biochemical Pharmacology, 1987 The sensitivity of the developing embryo to toxins and drugs is highly dependent on the state of development of the cytochrome P-450 system. Previous work in this laboratory has demonstrated the genotoxicity of aflatoxin B1 (AFB1) to the chicken embryo at 3 days of incubation (DI) and induction of AFB1 genotoxicity by phenobarbital at 7 DI.
Nancy A. Lorr, Stephen E. Bloom
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Model System Studies of Axial Ligation in the Oxidized Reaction States of Cytochrome P-450 Enzymes [PDF]
, 1976 Cytochrome P-450 enzymes have been isolated from bacteria, microsomes, and mitochondria and catalyze the insertion of one atom of dioxygen into substrate while the other is reduced to water. The biological and many of the physical properties of these enzymes are summarized elsewhere (Hill et al., 1970a; Ullrich, 1972; Gunsalus et al., 1973; Tomaszewski
R. H. Holm +6 more
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Journal of Lipid Research, 1981 The present study was undertaken to obtain information on the involvement of cytochrome P-450 in the 26-hydroxylation on bile acid intermediates and in the 25-hydroxylation of vitamin D3 in human liver mitochondria. Cytochrome P-450 was solubilized from human liver mitochondria and purified two times to a specific content of 0.125 nmol per mg protein ...
H Oftebro +3 more
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