Results 181 to 190 of about 1,703,947 (251)
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Hydroperoxide peroxidase activity in liver microsomes

Life Sciences, 1974
Abstract 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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A microsomal endoribonuclease from rat liver

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1980
An endoribonuclease has been purified about 320-fold from the microsomes of rat liver. The enzyme had an apparent molecular weight of 54 000-58 000 and produced oligonucleotides, each consisting of 3-7 nucleotides from poly(A) and poly(U). No mononucleotide was obtained by the enzymatic hydrolysis of poly(A) and poly(U) under standard coditions.
Seiyu Hirose   +5 more
openaire   +2 more sources

Stimulation of galactosyltransferase in liver microsomes by lysolecithin

Biochemical and Biophysical Research Communications, 1974
Abstract 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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THE MECHANISM OF SCHRADAN ACTIVATION BY LIVER MICROSOMES

Canadian Journal of Biochemistry and Physiology, 1957
The mechanism by which schradan is converted to a powerful anticholinesterase by fortified liver homogenates has been studied. A scheme is proposed involving the production from DPNH of hydrogen peroxide, which then oxidizes an unknown microsomal factor with the aid of catalase. The factor in turn oxidizes schradan.
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A microsomal exoribonuclease from rat liver

Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
Kazuei Igarashi   +4 more
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The interaction of cimetidine with rat liver microsomes

Biochemical Pharmacology, 1983
The binding of cimetidine to rat liver microsomes in M/15 phosphate buffer, pH 7.9, has been investigated by difference spectroscopy and also by equilibrium partition studies, the latter method providing the more definitive characterization of the interaction in the pharmacologically relevant, low micromolar range of drug concn. In addition, the effect
Reilly P.E.B.   +2 more
openaire   +4 more sources

Esterification of cholesterol in rat liver microsomes

Archives of Biochemistry and Biophysics, 1964
Washed rat liver microsomes esterify cholesterol in the presence of added ATP and CoA; net synthesis of cholesterol esters was demonstrated. The optimum pH of the reaction was between 6.8 and 7.2; the effects of time and concentration of substrate were investigated.
M.D. Law   +5 more
openaire   +3 more sources

Metabolism of doxophylline by rat liver microsomes.

Drug Metabolism and Disposition, 1986
The metabolic transformation of the bronchospasmolytic agent doxophylline (2-(7'-theophyllinemethyl)-1,3-dioxolane) was studied in vitro with phenobarbital-induced rat liver microsomal fraction containing the NADPH-generating system. Doxophylline was poorly metabolized as 95% of the recovered material was parent compound. The major metabolite resulted:
GROSA, Giorgio   +2 more
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Kavalactone Metabolism in Rat Liver Microsomes

Phytotherapy Research, 2011
The specific CYP enzymes involved in kavalactone (KLT) metabolism and their kinetics have not been fully examined. This study used rat liver microsomes (RLM) to determine kavain (KA), methysticin (MTS) and desmethoxyyangonin (DMY) enzyme kinetic parameters, to elucidate the major CYP450 isoforms involved in KLT metabolism and to examine gender ...
Anthony Rowe, Iqbal Ramzan, Shuang Fu
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The mechanism of liver microsomal lipid peroxidation

Biochimica et Biophysica Acta (BBA) - General Subjects, 1975
In the presence of Fe-3+ and complexing anions, the peroxidation of unsaturated liver microsomal lipid in both intact microsomes and in a model system containing extracted microsomal lipid can be promoted by either NADPH and NADPH : cytochrome c reductase or by xanthine and xanthine oxidase.
Steven D. Aust, Thomas C. Pederson
openaire   +3 more sources

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