Results 221 to 230 of about 104,306 (283)
, 1979 Stopped flow studies were undertaken to examine the kinetics of reduction of 5,6-benzoflavone-inducible P-450 LM4 by NADPH in the presence of NADPH-cytochrome P-450 reductase and phospholipid under anaerobic CO at 25 degrees C. The reaction exhibited biphasic kinetics irrespective of NADPH concentration or of the molar ratio of reductase to P-450 LM4 ...
K . P Vatsis, D . D Oprian, M. J Coon
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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
Hirofumi Shoun +2 more
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NADPH reduction of cytochrome P-450 at different integrational levels of the enzyme system
, 1979 The 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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The Cytochrome P-450 Drug Metabolizing Enzyme System
Journal of Head Trauma Rehabilitation, 2002 Bruno Wroblewski, Mel B. Glenn
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Neurotoxicology, 1984 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 alpha-, beta-, gamma- and delta-hydroxybutyldibutyltin derivatives.
Fish Rh
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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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Chapter 9 The Molecular Basis of Electron Transfer in Cytochrome P-450 Enzyme Systems
, 1992 Robert D. Gray
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