Results 261 to 270 of about 1,677,689 (317)
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Interaction of ranitidine with liver microsomes
Xenobiotica, 19821. Ranitidine interacts with liver microsomes from rats pretreated with different inducers of cytochrome P-450 to produce substrate difference optical spectra with a peak at 426-429 nm and a trough at 390-400 nm. 2. Cytochrome P-450 reduced with dithionite in the presence of ranitidine produced substrate difference spectra with a peak at 447 nm. 3.
S, Rendić +3 more
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Permeability of Liver Microsomal Membranes to Glucose
Biochemical and Biophysical Research Communications, 1996The permeability of rat liver microsomes to glucose has been studied by using (14)C-labelled D-glucose and a light-scattering technique. 1) The microsomal intravesicular apparent isotope space for D-glucose (1mM; after 5 min incubation at 22 degrees C) was 2.34 microl/mg protein, i.e., approximately 72% of the apparent water space.
MARCOLONGO, P. +4 more
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Mechanism of reduction of nitrofurantoin on liver microsomes
Pharmacological Research Communications, 1980Summary Reduction of the nitro-group of nitrofurantoin /N-[5-Nitro-2-furfuryliden-] 1-aminohydantoin/ on liver microsomes is supported both by NADPH and NADH. The site of interaction of nitrofurantoin with microsomes appears to be on two flavoproteins, NADPH-cytochrome P450 reductase and NADH-cytochrome b5 reductase; interaction with the former ...
M. Popović, V. Leskovac
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Chromate metabolism in liver microsomes
Biological Trace Element Research, 1979The carcinogenicity and mutagenicity of various chromium compounds have been found to be markedly dependent on the oxidation state of the metal. The carcinogen chromate was reduced to chromium(III) by rat liver microsomes in vitro. Metabolism of chromate by microsomal enzymes occurred only in the presence of either NADPH or NADH as cofactor.
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Development of immobilization technique for liver microsomes
Colloids and Surfaces B: Biointerfaces, 2009In the present report, physically adsorbed rat liver microsomes were used in order to optimize the immobilization of membrane proteins on solid surfaces for use in biosensing and microreactor applications. Physical adsorption was used to form thin films on solid supports (gold, mica, macroporous aluminum oxide membrane).
Tanvir, S. +3 more
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Chemical Research in Toxicology, 2008
In vitro covalent binding assessments of drugs have been useful in providing retrospective insights into the association between drug metabolism and a resulting toxicological response.
R. Obach +3 more
semanticscholar +1 more source
In vitro covalent binding assessments of drugs have been useful in providing retrospective insights into the association between drug metabolism and a resulting toxicological response.
R. Obach +3 more
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Activation of Thionophosphates by Liver Microsomes
Nature, 1959MANY organophosphorus insecticides are poor inhibitors of cholinesterase, but are converted to potent inhibitors (‘activated’) by certain mammalian and insect tissues. The activation by liver slices was first shown by Gardiner and Kilby1 for schradan (a phosphoroamidate), and by Diggle and Gage2 for parathion (a phosphorothionate). Davison3 showed that
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Microsomal antigens in developing chick liver
Experimental Cell Research, 1965Abstract Microsomes from embryonic and adult chick liver have been analyzed by homologous antisera. The deoxycholate-soluble fraction of embryonic microsomes contains a group of antigens typical to this fraction, but present only as a trace in the adult-homologous fraction.
E. Piazza, V. Mutolo, V. D'Amelio
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Hydroperoxide peroxidase activity in liver microsomes
Life Sciences, 1974Abstract The oxidation of either NADH or NADPH by cumene hydroperoxide in rat liver microsomes is described. The Km′ for the hydroperoxide varied with the pyridine nucleotide utilized (NADPH, Km′ = 0.91 mM; NADH, Km′ = 3.3 mM). Carbon monoxide did not inhibit the peroxidase activity although a variety of other agents which interact with cytochrome ...
Paul Hochstein, Wayne R. Bidlack
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Stimulation of galactosyltransferase in liver microsomes by lysolecithin
Biochemical and Biophysical Research Communications, 1974Abstract Lysolecithin markedly stimulated membrane-bound UDP-galactose:glycoprotein galactosyltransferase. The parent molecule lecithin, phosphatidylethanolamine, lysophosphatidylethanolamine, phosphatidic acid, lysophosphatidic acid or glycerophosphorylcholine did not activate the enzyme suggesting that both fatty acyl- and phosphorylcholine groups ...
James W.M. Yung, Sailen Mookerjea
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