Results 191 to 200 of about 102,281 (237)
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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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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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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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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
N,N-Dimethylaniline when added to reaction mixtures provokes deviation from Michaelis-Menten law of the interaction kinetics of NADPH-cytochrome c(P-450) reductase (NADPH:ferrihaemoprotein oxidoreductase, EC 1.6.2.4) with highly purified phenobarbital-induced rabbit liver microsomal cytochrome P-450 (P-450LM2).
P, Hlavica, I, Golly, J, Wolf
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N,N-Dimethylaniline when added to reaction mixtures provokes deviation from Michaelis-Menten law of the interaction kinetics of NADPH-cytochrome c(P-450) reductase (NADPH:ferrihaemoprotein oxidoreductase, EC 1.6.2.4) with highly purified phenobarbital-induced rabbit liver microsomal cytochrome P-450 (P-450LM2).
P, Hlavica, I, Golly, J, Wolf
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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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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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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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Chemosphere, 1992
Abstract In the present study, in vitro effects of carcinogenic (chrysotile, crocidolite, amosite) and non-carcinogenic (anthophyllite) varieties of asbestos and three varieties of Indian wollastonite (kemolit A-60, Kemolit-N, Kemolit ASB-3) boTh on phase I and phase Ii drug metabolizing enzymes and microsomal lipid peroxidatin (LPO) in rat lung were
Sikandar G. Khan, S. Ali, Q. Rahman
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Abstract In the present study, in vitro effects of carcinogenic (chrysotile, crocidolite, amosite) and non-carcinogenic (anthophyllite) varieties of asbestos and three varieties of Indian wollastonite (kemolit A-60, Kemolit-N, Kemolit ASB-3) boTh on phase I and phase Ii drug metabolizing enzymes and microsomal lipid peroxidatin (LPO) in rat lung were
Sikandar G. Khan, S. Ali, Q. Rahman
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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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