Search results for "Cytochrome P-450 Enzyme System"

showing 10 items of 163 documents

Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450.

1989

The phosphorylation of the two major phenobarbital-inducible cytochrome P450 isoenzymes IIB1 and IIB2 was increased in hepatocytes by the action of the membrane permeating cAMP derivatives N6-dibutyryl-cAMP and 8-thiomethyl-cAMP. Under these conditions the dealkylation of 7-pentoxyresorufin, a selective substrate of cytochrome P450IIB1 and P450IIB2 was markedly reduced. 16 beta-Hydroxylation of testosterone which is catalyzed specifically only by cytochrome P450IIB1 and IIB2 was strongly reduced; for 16 alpha-hydroxylation which is also catalyzed by cytochrome P450IIB1 and IIB2 but additionally by 3 further cytochrome P450 isoenzymes, this reduction was less pronounced; for the oxidation of…

MaleCytochromeStereochemistry25-Hydroxyvitamin D3 1-alpha-hydroxylaseBiophysicsHydroxylationBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemCyclic AMPCytochrome c oxidaseAnimalsTestosteronePhosphorylationMolecular BiologybiologyChemistryCytochrome c peroxidaseCytochrome cCYP1A2Cytochrome P450 reductaseRats Inbred StrainsCell BiologyRatsIsoenzymesBiochemistryLiverSteroid 16-alpha-HydroxylaseCoenzyme Q – cytochrome c reductasePhenobarbitalbiology.proteinProtein Processing Post-TranslationalBiochemical and biophysical research communications
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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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Metabolism of apigenin by rat liver phase I and phase II enzymes and by isolated perfused rat liver

2004

The metabolism of apigenin, a low estrogenic flavonoid phytochemical, was investigated in rat using liver models both in vitro (subcellular fractions) and ex vivo (isolated perfused liver). In vitro, phase I metabolism led to the formation of three monohydroxylated derivatives: luteolin which was the major metabolite (K(m) = 22.5 +/- 1.5 microM; V(max) = 5.605 +/- 0.090 nmol/min/mg protein, means +/- S.E.M.), scutellarein, and iso-scutellarein. These oxidative pathways were mediated by cytochrome P450 monooxygenases (P450s). The use of P450 inhibitors and inducers showed that CYP1A1, CYP2B, and CYP2E1 are involved. In vitro studies of phase II metabolism indicated that apigenin underwent co…

MaleFMN ReductaseMetabolite[SDV]Life Sciences [q-bio]Pharmaceutical ScienceIn Vitro TechniquesMethylation030226 pharmacology & pharmacyMass Spectrometry03 medical and health scienceschemistry.chemical_compoundGlucuronides0302 clinical medicineCytochrome P-450 Enzyme SystemAnimalsApigeninEnzyme InhibitorsRats WistarLuteolinBiotransformationChromatography High Pressure LiquidComputingMilieux_MISCELLANEOUS030304 developmental biologyFlavonoidsPharmacologySex Characteristics0303 health sciencesbiologySulfatesScutellareinCytochrome P450MonooxygenaseDiosmetinRats3. Good health[SDV] Life Sciences [q-bio]KineticsLiverBiochemistrychemistryApigeninbiology.proteinRATFemaleSpectrophotometry UltravioletLuteolinNADPDrug metabolismSubcellular Fractions
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Modification of hepatic drug-metabolizing enzymes in rat fed naturally occurring allyl sulphides

1994

1. The effects of feeding allyl sulphides to rat (2000 ppm of the diet for 15 days) were investigated on various microsomal hepatic drug-metabolizing enzymes by their immunochemical detection and catalytic activity. 2. Allyl sulphides provoked a temporary dietary restriction, which enhanced the microsomal level of P450 and the activities of NADH-cytochrome c reductase and p-hydroxybiphenyl UDP-glucuronyltransferase (UDPGT 2), and lowered the activities of p-nitrophenol hydroxylase (PNPH), N-nitrosodimethylamine demethylase (NDMAD), laurate omega-hydroxylase (LAH) and glutathione S-transferase (GST). Therefore, pair-fed animals were used as a more relevant control for the dietary effects of …

MaleHealth Toxicology and MutagenesisImmunoblottingAllyl compoundAntineoplastic Agents[SDV.BID]Life Sciences [q-bio]/BiodiversitySulfidesReductaseToxicologyBiochemistryEating03 medical and health scienceschemistry.chemical_compound0302 clinical medicineIMMUNOCHIMIECytochrome P-450 Enzyme SystemAnimalsDisulfidesGlucuronosyltransferaseRats WistarEpoxide hydrolaseAnticarcinogenGlutathione Transferase030304 developmental biologyEpoxide HydrolasesPharmacologychemistry.chemical_classification0303 health sciencesDose-Response Relationship DrugbiologyChemistryBody WeightCytochrome P450Organ SizeGeneral MedicineGlutathioneDietRatsAllyl CompoundsEnzymeLiverBiochemistryTOXICOLOGIE030220 oncology & carcinogenesisMicrosomes Liverbiology.proteinMicrosomeRAT[SDV.BID] Life Sciences [q-bio]/Biodiversity
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A novel haemoprotein induced by isosafrole pretreatment in the rat

1978

Abstract Sodium dodecyl sulphate-polyacrylamide gel electrophoresis has been used to demonstrate that pretreatment of rats with isosafrole results in the formation of a novel species of cytochrome P-450 (mol. wt. 54,000) quite distinct from that induced by phenobarbitone pretreatment (mol. wt. 50,000) or 3-methylcholanthrene (mol. wt. 58,000).

MaleHemeproteinCytochromeSodiumBiophysicschemistry.chemical_elementDioxolesBiochemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemIsomerismSafroleMoleAnimalsMolecular BiologyGel electrophoresisChromatographybiologyChemistrySpectrum AnalysisCell BiologyRatsMolecular WeightBiochemistryIsosafroleEnzyme InductionPhenobarbitalMicrosomes Liverbiology.proteinApoproteinsMethylcholanthreneBiochemical and Biophysical Research Communications
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Cryopreservation of rat, dog and human hepatocytes: influence of preculture and cryoprotectants on recovery, cytochrome P450 activities and induction…

2006

Several cryopreservation protocols for hepatocytes have been proposed over the past few years, but their effectiveness varies greatly as a function of the characteristics of the method used. One factor in the success of cryopreservation is the quality of cells before freezing. The results suggest that the cryopreservation of hepatocytes in a medium containing polyvinylpyrrolidone (PVP), in addition to DMSO, constitutes a convenient means of long-term storage of hepatocytes for preparing primary cultures to be used in drug metabolism studies. The combined use of the two cryoprotectants is particularly critical for low-viability cell suspensions. An interesting alternative to increase cell vi…

MaleHot TemperatureCryoprotectantHealth Toxicology and MutagenesisCellCombined useDrug Evaluation PreclinicalToxicologyBiochemistryCryopreservationRats Sprague-DawleyCryoprotective AgentsDogsCytochrome P-450 Enzyme SystemmedicineAnimalsHumansDimethyl SulfoxideViability assayCells CulturedCryopreservationPharmacologybiologyPovidoneCytochrome P450General MedicineRatsCell biologyEnzyme Activationmedicine.anatomical_structureBiochemistryHepatocytesbiology.proteinDrug metabolismXenobiotica
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On the spectral intermediate at 440 nm formed during mixed function substrate oxidation.

1974

Abstract The spectral shoulder formed at 440 nm in microsomes oxidising hexobarbital and other drugs has been investigated and some of its properties characterised. Hexobarbital, pentobarbital, ethylmorphine and barbital produce this shoulder, while acetanilide, aniline, desmethylimipramine, imipramine, metyrapone and SKF 525-A do not. The formation of the 440 nm shoulder depends on the presence of NADPH and oxygen and is reduced in size when NADH is also present. At saturating substrate concentrations the size of the 440 nm shoulder is correlated to the cytochrome P-450 content. The hexobarbital induced shoulder can be inhibited by drug metabolism inhibitors such as metyrapone, imipramine …

MaleImipramineCytochromeStereochemistrychemistry.chemical_elementBarbitalIn Vitro TechniquesPhotochemistryBiochemistryOxygenMixed Function Oxygenaseschemistry.chemical_compoundAnilineOxygen ConsumptionCytochrome P-450 Enzyme SystemmedicineAnimalsAcetanilidePentobarbitalPharmacologyAniline CompoundsbiologyProadifenDesipramineSubstrate (chemistry)MetyraponeEthylmorphineNADRatsKineticsHexobarbitalchemistryMorphinansBarbituratesbiology.proteinMicrosomes LiverAcetanilidesSpectrophotometry UltravioletOxidoreductasesOxidation-ReductionNADPmedicine.drugProtein BindingBiochemical pharmacology
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