Search results for "Microsome"

showing 10 items of 262 documents

Induction of rat hepatic epoxide hydratase by dietary antioxidants

1979

Abstract Supplementation of rat diet with butylated hydroxytoluene (BHT), butylated hydroxyanisole, or ethoxyquin resulted in increased liver epoxide hydratase activity. The increase was obvious at 0.1% and amounted to 200–400% at 0.5%. Increased activity was accompanied by increased proportion of the epoxide hydratase band in SDS polyacrylamide gels, indicating induction of the enzyme. Ethoxycoumarin deethylase activity and cytochrome b5 concentrations were moderately elevated while cytochrome P-450 concentrations and aryl hydrocarbon hydroxylase activity remained at control levels. Preferential inhibition of monooxygenase activity by metyrapone and not 7,8-benzoflavone, as well as increas…

MaleCytochromePopulationThymus GlandToxicologyAntioxidantsMixed Function Oxygenaseschemistry.chemical_compoundCytochrome b5AnimalsButylated hydroxytolueneDrug InteractionsBenzopyreneseducationEpoxide HydrolasesPharmacologychemistry.chemical_classificationeducation.field_of_studyEthoxyquinbiologyChemistryDNADietRatsEnzymeLiverBiochemistryEnzyme InductionMicrosomebiology.proteinButylated hydroxyanisoleToxicology and Applied Pharmacology
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Oxidation of tienilic acid by human yeast-expressed cytochromes P-450 2C8, 2C9, 2C18 and 2C19. Evidence that this drug is a mechanism-based inhibitor…

1996

Oxidation of tienilic acid by human cytochromes P-450 (CYP) 2C9, 2C18, 2C8 and 2C19 was studied using recombinant enzymes expressed in yeast. CYP 2C9 was the best catalyst for 5-hydroxylation of tienilic acid (K(m) = 5 +/- 1 microM, kcat = 1.7 +/- 0.2 min-1), 30-fold more potent in terms of kcat/K(m) than CYP 2C18 (K(m) = 150 +/- 15 microM, kcat = 1.8 +/- 0.2 min-1) and 300-fold more potent than CYP 2C8 (K(m) = 145 +/- 15 microM, kcat = 0.2 +/- 0.1 min-1). CYP 2C19 was unable to catalyze this hydroxylation under our experimental conditions. During this study, a marked effect of the ionic strength on the activities (hydroxylations of tienilic acid and tolbutamide) of these cytochromes P-450 …

MaleCytochromeTolbutamideTicrynafenSaccharomyces cerevisiaeurologic and male genital diseasesHydroxylationBiochemistryMixed Function OxygenasesHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemMicrosomesmedicineCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme InhibitorsCytochrome P-450 Enzyme Inhibitorschemistry.chemical_classificationbiologyChemistryorganic chemicalsMembrane ProteinsGlutathionerespiratory systemRecombinant ProteinsIsoenzymesenzymes and coenzymes (carbohydrates)EnzymeBiochemistrySteroid 16-alpha-HydroxylaseTienilic acidSuicide inhibitionbiology.proteinMicrosomeMicrosomes LiverAryl Hydrocarbon HydroxylasesOxidation-Reductionmedicine.drugEuropean journal of biochemistry
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Ethoxyquin as an inducer and inhibitor of phenobarbital-type cytochrome P-450 in rat liver microsomes.

1977

Abstract The effect of ethoxyquin in vivo and in vitro on drug metabolism in rat liver microsomes was studied. In feeding experiments, a threshold dose of induction was found at 0.05% ethoxyquin for 14 days. At 0.5% ethoxyquin, relative liver weight, cytochrome P-450 content, cytochrome b5 content, ethylmorphine demethylation, and ethoxycoumarin deethylation were increased by a factor of 1.5 to 2. Aryl hydrocarbon hydroxylase activity was, however, not induced but even decreased by 0.5% ethoxyquin in food. Induction of epoxide hydratase was marked, amounting to 400% of control after 0.5% ethoxyquin. The induced enzyme was similar to the phenobarbital-inducible cytochrome P-450 in its CO spe…

MaleCytochromeToxicologyMixed Function OxygenasesHydroxylationchemistry.chemical_compoundEthoxyquinCytochrome P-450 Enzyme SystemCytochrome b5AnimalsCytochrome P-450 Enzyme InhibitorsDemethylationPharmacologyEthoxyquinbiologyChemistryOrgan SizeMonooxygenaseRatsBiochemistryEnzyme InductionPhenobarbitalMicrosomebiology.proteinMicrosomes LiverQuinolinesElectrophoresis Polyacrylamide GelDrug metabolismToxicology and applied pharmacology
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Properties of the microsomal and cytosolic glutathione transferases involved in hexachloro-1:3-butadiene conjugation

1989

Hexachloro-1,3-butadiene (HCBD) is a substrate for the hepatic microsomal glutathione transferases and is metabolised at higher rates by these enzymes than their cytosolic counterparts. Conjugation reactions catalysed by the microsomal and cytosolic transferases have been studied and characterized using this substrate and 1-chloro-2,4-dinitrobenzene (CDNB). In rat liver microsomes the Km values for HCBD and CDNB were 0.91 and 0.012 mM and in cytosol 0.51 and 0.10 mM respectively. Vmax values for HCBD were 1.39 and 0.35 nmol conjugate formed/min/mg protein for microsomes and cytosol respectively. In microsomal systems HCBD was a potent competitive inhibitor of the metabolism of CDNB with a K…

MaleDetergentsGuinea PigsCholic AcidBiochemistrySulfobromophthaleinchemistry.chemical_compoundCytochrome P-450 Enzyme SystemCricetinaeButadienesDinitrochlorobenzeneAnimalsHumansGlutathione transferase activityGlutathione TransferasePharmacologychemistry.chemical_classificationbiologyEndoplasmic reticulumBilirubinCholic AcidsGlutathioneMetabolismbiology.organism_classificationRatsKineticsCytosolEnzymeSolubilitychemistryBiochemistryMicrosomaMicrosomes LiverMicrosomeRabbitsBiochemical Pharmacology
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Effect of unbalanced diets on incorporation of δ-aminolevulinic acid into cytochrome P-450

1987

Abstract The in vivo syntheses of two liver microsomal cytochromes P-450 PB 3a , P-450 UT 50 [(1987) Eur. J. Biochem., submitted] ( M r 50 000, 52 000) have been estimated by measuring the specific activity 2 h after i.p. administration of δ-[ 3 H]aminolevulinic acid to male Sprague Dawley rats. The animals were fed either a standard rat chow (5% lard, 22% casein) or unbalanced diets (high lipid, 30% lard or low protein, 6% casein) with or without 50 ppm Phenoclor DP6. The high-lipid diet supported a more rapid body weight gain but had little impact on cytochrome P-450 content, expressed either per whole liver or per mg microsomal protein, and on the incorporation of the precursor into cyto…

MaleDietary proteinLow proteinCytochromeBiophysicsPolychlorobiphenylBiochemistryIsozymeδ-Aminolevulinic acidchemistry.chemical_compoundCytochrome P-450 Enzyme SystemNutritional effectStructural BiologyIn vivoCaseinGeneticsAnimalsCelluloseMolecular BiologyChromatographybiologyRats Inbred StrainsAminolevulinic AcidCell BiologyLevulinic AcidsDietRatsLiverchemistryBiochemistryCytochrome P-450 synthesisMicrosomebiology.proteinSpecific activityFEBS Letters
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Visualization of a covalent intermediate between microsomal epoxide hydrolase, but not cholesterol epoxide hydrolase, and their substrates

1997

Mammalian soluble and microsomal epoxide hydrolases have been proposed to belong to the family of alpha/beta-hydrolase-fold enzymes. These enzymes hydrolyse their substrates by a catalytic triad, with the first step of the enzymatic reaction being the formation of a covalent enzyme-substrate ester. In the present paper, we describe the direct visualization of the ester formation between rat microsomal epoxide hydrolase and its substrate. Microsomal epoxide hydrolase was precipitated with acetone after brief incubation with [1-(14)C]epoxystearic acid. After denaturing SDS gel electrophoresis the protein-bound radioactivity was detected by fluorography. Pure epoxide hydrolase and crude micros…

MaleEpoxide hydrolase 21303 BiochemistryStereochemistryMolecular Sequence DataEpoxide10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiochemistryRats Sprague-Dawleychemistry.chemical_compoundCatalytic triadAnimalsAmino Acid SequenceEpoxide hydrolaseMolecular BiologyEpoxide Hydrolaseschemistry.chemical_classificationHydrolysisCell BiologyRatsKineticsCholesterolEnzymeModels ChemicalSolubilitychemistryBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesCarcinogensChromatography GelMicrosomes LiverMicrosomeEpoxy Compounds570 Life sciences; biologySequence AlignmentStearic Acids
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Induction of rat liver microsomal epoxide hydrolase by its endogenous substrate 16α, 17α-epoxyestra-1,3,5-trien-3-ol

1995

1. The influence of the endogenous steroid epoxides 16 alpha, 17 alpha-epoxyestra-1,3,5(10)-trien-3-ol (estroxide) and 16 alpha, 17 alpha-expoxiandrost-4-en-3-one (androstene oxide) and their metabolic precursors estra-1,3,5(10), 16-tetraen-3-ol (estratetraenol) and androsta-4, 16-dien-3-one (androstadienone) on the specific activities of hepatic microsomal and soluble epoxide hydrolase, glutathione S-transferase, dihydrodiol dehydrogenase, and 7-ethoxycoumarin deethylase was investigated in the male Sprague-Dawley rat. 2. Both estroxide and estratetraenol induced microsomal epoxide hydrolase activity towards styrene oxide and estroxide itself 2-2.5-fold and glutathione conjugation of 1-chl…

MaleEpoxide hydrolase 2Health Toxicology and Mutagenesis7-Alkoxycoumarin O-DealkylaseToxicologyBiochemistryRats Sprague-Dawleychemistry.chemical_compoundEstratetraenolStyrene oxideAnimalsEpoxide hydrolaseGlutathione TransferaseEpoxide HydrolasesPharmacologyEstriolChemistryAndrostadienoneGeneral MedicineGlutathioneRatsBiochemistryEnzyme InductionMicrosomal epoxide hydrolaseMicrosomes LiverMicrosomeEpoxy CompoundsOxidoreductasesXenobiotica
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Ethoxyquin feeding to rats increases liver microsome-catalyzed formation of benzo(a)pyrene diol epoxide--DNA adduct.

1978

Abstract The ability of rat liver microsomes to catalyze the formation of benzo(a)pyrene 7,8-diol-9,10-epoxide — DNA nucleoside adduct was increased threefold by feeding 0.5% ethoxyquin to the animals. Microsomal epoxide hydratase activity was enhanced i parallel by a factor of 3 while aryl hydrocarbon hydroxylase activity was not induced. Liver microsomes from rat pretreated with 3-methylcholanthrene produced an increased proportion of diol epoxide — DNA adduct when ethoxyquin had been fed to the animals. The main chromatographic peak formed by microsomes from 3-methylcholanthrene treated rats which contains DNA adducts of secondary benzo(a)pyrene phenol metabolites is reduced when the ani…

MaleEthoxyquinChemistryBiophysicsEpoxideCell BiologyDNABiochemistryAdductRatschemistry.chemical_compoundEthoxyquinBiochemistryBenzo(a)pyreneDNA adductMethylcholanthreneMicrosomeMicrosomes LiverQuinolinesPyreneAnimalsEpoxy CompoundsBenzopyrenesMolecular BiologyMethylcholanthreneBiochemical and biophysical research communications
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Effect of dietary antioxidants on benzo[a]pyrene metabolism in rat liver microsomes

1983

Feeding of rats with 1% ethoxyquin (EQ) and butylated hydroxytoluene (BHT) but not butylated hydroxyanisole (BHA) increases the formation rate of benzo[a]pyrene (BP)-4,5-dihydrodiol from BP in hepatic microsomes. The production of other BP-dihydrodiols and of BP phenols is decreased after treatment with EQ, BHT and BHA. EQ and BHT are more effective than BHA in inducing epoxide hydrolase (EH) activity towards styrene oxide as the substrate.

MaleEthoxyquinRats Inbred StrainsButylated HydroxytolueneIn Vitro TechniquesToxicologyAntioxidantsRatschemistry.chemical_compoundEthoxyquinchemistryBenzo(a)pyreneBiochemistryStyrene oxideBenzo(a)pyreneCarcinogensMicrosomes LiverAnimalsPyreneButylated hydroxytoluenePhenolsFood scienceBenzopyrenesButylated hydroxyanisoleEpoxide hydrolaseToxicology
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CHARACTERIZATION OF MICROSOMAL CYTOCHROME P450-DEPENDENT MONOOXYGENASES IN THE RAT OLFACTORY MUCOSA

2005

Nasal administration of a drug ensures therapeutic action by rapid systemic absorption and/or the entry of some molecules into the brain through different routes. Many recent studies have pointed out the presence of xenobiotic-metabolizing enzymes in rat olfactory mucosa (OM). Nevertheless, very little is known about the precise identity of isoforms of cytochrome P450 (P450)-dependent monooxygenases (P450) and their metabolic function in this tissue. Therefore, we evaluated mRNA expression of 19 P450 isoforms by semiquantitative reverse transcriptase-polymerase chain reaction and measured their microsomal activity toward six model substrates. For purposes of comparison, studies were conduct…

MaleGene isoformPharmaceutical ScienceOlfactionSubstrate SpecificityOlfactory mucosaOlfactory MucosaMicrosomesmedicineAnimalsRNA MessengerEnzyme InhibitorsRats WistarPharmacologychemistry.chemical_classificationbiologyReverse Transcriptase Polymerase Chain ReactionCYP1A2Cytochrome P450MonooxygenaseRatsIsoenzymesKineticsEnzymemedicine.anatomical_structureBiochemistrychemistryMicrosomes Liverbiology.proteinMicrosomeAryl Hydrocarbon HydroxylasesDrug Metabolism and Disposition
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