Results 111 to 120 of about 27,503 (167)
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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 ...
W R, Bidlack, P, Hochstein
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A microsomal endoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1980An 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.
H, Kumagai +5 more
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Ethylene Formation in Rat Liver Microsomes
Science, 1966Reduced triphosphopyridine nucleotide and pyrophosphate-dependent peroxidation of lipids in rat liver microsomes were coupled to the generation of ethylene in the presence of cuprous ions. This system suggests a model for the biogenesis of ethylene in cells.
M, Lieberman, P, Hochstein
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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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Pigments of rat liver microsomes
Archives of Biochemistry and Biophysics, 1958Abstract The total hemin content of washed rat liver microsomes is 2.15 times the cytochrome b5 content, only a small part being due to bound hemoglobin. The content of flavine is 4 5 that of cytochrome b5. The flavine probably does not contribute to the DPNH reduced difference spectrum.
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Kavalactone Metabolism in Rat Liver Microsomes
Phytotherapy Research, 2011The 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 ...
Shuang, Fu, Anthony, Rowe, Iqbal, Ramzan
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FRACTIONATION OF MOUSE LIVER MICROSOMAL ESTERASES
Canadian Journal of Biochemistry, 1965Mouse liver microsomal esterases were fractionated on DEAE-cellulose after the solution of these enzymes in a solution containing 0.1 M glycyl glycine buffer, pH 7.0, and 5 × 10−4 M Lubrol W, a nonionic detergent. Elution of the enzymes from the DEAE-cellulose was accomplished by using NaCl in the glycyl glycine – Lubrol W solution.
C, CARRUTHERS, E, HEINS, A, BAUMLER
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A microsomal exoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979A 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.
H, Kumagai +4 more
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Lipid peroxidation of rat liver microsomes
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 19801. The NADPH-dependent lipid peroxidation process was studied with microsomes and also the effects of addition of superoxide dismutase, catalase and thiourea. Only catalase and thiourea were able to inhibit lipid peroxidation. It seems that the initiating radical is the OH. radical formed by the Fenton reaction. 2.
J F, Koster, R G, Slee
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Mannosyltransfer reactions in rabbit liver microsomes
Biochemical and Biophysical Research Communications, 1976Abstract Rabbit liver microsomes catalyzed mannosyltransfer from GDP-[14C]mannose to free D -mannose resulting in the synthesis of α-1,2-, α-1,3-, and α-1,6-mannosyl-mannose. Whereas formation of α-1,2-mannosyl-mannose was stimulated by the addition of manganese chloride or nickel chloride and was inhibited by EDTA, synthesis of α-1,3-mannosyl ...
J S, Schutzbach, A K, Verma
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