Results 221 to 230 of about 42,048 (270)
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Journal of Environmental Science and Health, Part B, 1981
Livers of mice previously treated with potential inducers were tested for effects on the microsomal cytochrome P-450-dependent monooxygenase system (including its constituent electron transport enzymes) and other enzymes. Microsomes were also examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
K M, Robacker, A P, Kulkarni, E, Hodgson
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Livers of mice previously treated with potential inducers were tested for effects on the microsomal cytochrome P-450-dependent monooxygenase system (including its constituent electron transport enzymes) and other enzymes. Microsomes were also examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
K M, Robacker, A P, Kulkarni, E, Hodgson
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SECRETION OF MEDULLIPIN I BY THE KIDNEY INVOLVES THE CYTOCHROME P-450 ENZYME SYSTEM
Journal of Hypertension, 1994To determine whether secretion of medullipin I by the kidney is dependent on the cytochrome P-450 enzyme system in Sprague-Dawley and spontaneously hypertensive rats (SHR).Isolated kidneys from Sprague-Dawley rats were perfused with 5% human albumin gassed with 95% O2 and 5% CO2 at 185 mmHg. The resultant renal venous effluent was tested in the SHR for
E E, Muirhead, B, Brooks, L W, Byers
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Inhalation of Butanols: Changes in the Cytochrome P-450 Enzyme System
1985After inhalation of different butanol isomers for 3 days (2000 ppm) and 5 days (500 ppm), liver and kidney parameters of the microsomal cytochrome P-450 enzyme system were increased. sec-Butanol caused the highest increase in cytochrome P-450 concentration with a 47% rise in the kidneys (500 ppm for 5 days) and 33% in the liver (2000 ppm for 3 days). A
K, Aarstad, K, Zahlsen, O G, Nilsen
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Biochemical and Biophysical Research Communications, 1981
Abstract Cytochrome P-450 from liver microsomes of phenobarbital-treated rabbits catalyzed anaerobic dehalogenation of halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) when combined with NADPH and NADPH-cytochrome P-450 reductase. Cytochromes P-450B1 and P-448 from liver microsomes of untreated rabbits were less active. Triton X-100 accelerated the
K, Fujii +5 more
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Abstract Cytochrome P-450 from liver microsomes of phenobarbital-treated rabbits catalyzed anaerobic dehalogenation of halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) when combined with NADPH and NADPH-cytochrome P-450 reductase. Cytochromes P-450B1 and P-448 from liver microsomes of untreated rabbits were less active. Triton X-100 accelerated the
K, Fujii +5 more
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Enzyme, 2017
The rate of oxidative déméthylation of ethylmorphine by preparations of microsomes from livers of male rats decreased following whole-body γ-irradiation, reaching a minimum of 50% of the control value on the 5th or 6th day. The value of apparent V(max) changed markedly after irradiation when the K(m) value was unaltered. At the same time, the amount of
J M, Zajac, P, Bernard
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The rate of oxidative déméthylation of ethylmorphine by preparations of microsomes from livers of male rats decreased following whole-body γ-irradiation, reaching a minimum of 50% of the control value on the 5th or 6th day. The value of apparent V(max) changed markedly after irradiation when the K(m) value was unaltered. At the same time, the amount of
J M, Zajac, P, Bernard
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Analytica Chimica Acta, 1991
Abstract A number of staining techniques on Western blots were compared with respect to sensitivity, background staining and practical applicability. After electrophoresis of a rat microsomal preparation, followed by blotting and incubation of a primary antibody against a purified cytochrome P-450 fraction, enzyme-labelled second antibodies were used
Jansen, EHJM +3 more
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Abstract A number of staining techniques on Western blots were compared with respect to sensitivity, background staining and practical applicability. After electrophoresis of a rat microsomal preparation, followed by blotting and incubation of a primary antibody against a purified cytochrome P-450 fraction, enzyme-labelled second antibodies were used
Jansen, EHJM +3 more
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NADPH reduction of cytochrome P-450 at different integrational levels of the enzyme system
1979The complex monooxygenatic enzyme exhibits different functional behaviour at different integrational levels, thus indicating distinct organizational states. The aerobic NADPH reduction of microsomes, solubilized and reconstituted systems follows a biphasic kinetics, the two phases are attributed to associated state (cluster) and random cytochrome P-450
J, Blanck +5 more
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Journal of Organometallic Chemistry, 1976
Abstract The biological oxidation of several tributyltin derivatives, by a cytochrome P-450 dependent monooxygenase enzyme system with reduced nicotinamideadeninedinucleotidephosphate as the essential cofactor, produced carbon-hydroxylated compounds identified as α-, β-, γ- and δ-hydroxybutyldibutyltin derivatives.
Richard H. Fish +2 more
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Abstract The biological oxidation of several tributyltin derivatives, by a cytochrome P-450 dependent monooxygenase enzyme system with reduced nicotinamideadeninedinucleotidephosphate as the essential cofactor, produced carbon-hydroxylated compounds identified as α-, β-, γ- and δ-hydroxybutyldibutyltin derivatives.
Richard H. Fish +2 more
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Toxicology Letters, 1982
The N- and ring-hydroxylation of 2-acetylaminofluorene (AAF) are examined with a reconstituted cytochrome P-450 enzyme system from liver microsomal fractions from both control and 3-methylcholanthrene (MC)-pretreated mice. Partial purification of cytochrome P-450 fraction is achieved by bacterial protease treatment of microsomes followed by Triton X ...
P D, Lotlikar, T F, Wang
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The N- and ring-hydroxylation of 2-acetylaminofluorene (AAF) are examined with a reconstituted cytochrome P-450 enzyme system from liver microsomal fractions from both control and 3-methylcholanthrene (MC)-pretreated mice. Partial purification of cytochrome P-450 fraction is achieved by bacterial protease treatment of microsomes followed by Triton X ...
P D, Lotlikar, T F, Wang
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The Journal of Biochemistry, 1985
The cell-free extract of a cytochrome P-450-producing fungus, Fusarium oxysporum, was found to catalyze the hydroxylation of fatty acids. Three product isomers were formed from a single fatty acid. The products from lauric acid were identified by mass-spectrometry as 9-, 10-, and 11-hydroxydodecanoic acids, and those from palmitic acid as 13-, 14-, and
H, Shoun, Y, Sudo, T, Beppu
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The cell-free extract of a cytochrome P-450-producing fungus, Fusarium oxysporum, was found to catalyze the hydroxylation of fatty acids. Three product isomers were formed from a single fatty acid. The products from lauric acid were identified by mass-spectrometry as 9-, 10-, and 11-hydroxydodecanoic acids, and those from palmitic acid as 13-, 14-, and
H, Shoun, Y, Sudo, T, Beppu
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