Search results for "microsomes"

showing 10 items of 193 documents

Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

1984

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drugBiochemical and Biophysical Research Communications
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NADPH-cytochrome P-450 reductase: Preferential inhibition by ellipticine and other type II compounds having little effect on NADPH-cytochrome c reduc…

1980

Abstract Ellipticine (5,11-dimethyl-[6H]-pyrido[4,3b]carbazole) binds with an affinity greater than most other compounds known to interact with P-450. Control and 3-methylcholanthrene-induced aryl hydrocarbon (benzo[ a ]pyrene) hydroxylase (EC 1.14.14.2) and acetanilide 4-hydroxylase and control and phenobarbital-induced ethylmorphine N -demethylase activities are all markedly inhibited by ellipticine to about the same extent. Ellipticine and other Type II compounds (metyrapone, octylamine-1, pyridine and aniline) preferentially inhibit NADPH-cytochrome P-450 reductase activity, while affecting NADPH-cytochrome c reductase activity very little. Butanol-1, a compound having pure Reverse Type…

CytochromeStereochemistryIn Vitro TechniquesReductaseBiochemistryMixed Function OxygenasesMicechemistry.chemical_compoundAlkaloidsCytochrome P-450 Enzyme SystemAnimalsEllipticinesBenzopyrenesBinding siteAcetanilideNADPH-Ferrihemoprotein ReductasePharmacologychemistry.chemical_classificationbiologyCytochrome cDNAElectron acceptorchemistryMicrosomes Liverbiology.proteinMicrosomePyreneBiochemical Pharmacology
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Kinetic experiments on the binding of metyrapone to liver microsomes

1969

Kinetic experiments on the inhibition of oxidative microsomal O- and N-demethylations by metyrapone (2-methyl-1, 2-bis(3-pyridyl)-l-propanone, Su 4885) were carried out using mouse liver microsomes as the enzyme source. The model substrates were p-nitroanisole and N-monomethyl-p-nitroaniline. It was shown that the inhibition is competitive. The K i for metyrapone is 0.42 × 10−4 M and for the reduced metabolite of metyrapone 1.15×10−4 M. Their spectral dissooiation constants as determined from difference spectra have almost the same values. From this it is concluded that the degree of inhibition is correlated to the amount of metyrapone bound to cytochrome P-450. Metyrapone does not seem to …

CytochromeStereochemistryMetaboliteMixed Function OxygenasesNitrophenolsMicechemistry.chemical_compoundNon-competitive inhibitionmedicineAnimalsBinding siteBiotransformationPharmacologyAniline CompoundsBinding SitesMetyraponebiologyChemistryProadifenSubstrate (chemistry)General MedicineMetyraponeReceptor–ligand kineticsKineticsBiochemistryMicrosomes LiverMicrosomebiology.proteinCytochromesmedicine.drugNaunyn-Schmiedebergs Archiv f�r Pharmakologie
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Cytoplasmic autoantigens in autoimmune hepatitis: molecular analysis and clinical relevance.

1991

CytoplasmHepatologybusiness.industryAutoimmune hepatitismedicine.diseaseAutoantigensMolecular analysisAutoimmune DiseasesHepatitisCytosolCytoplasmMicrosomesImmunologymedicineHumansClinical significancebusinessAutoantibodiesSeminars in liver disease
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Biomarker responses of the earthworm Aporrectodea tuberculata to copper and zinc exposure: differences between populations with and without earlier m…

2003

Biomarkers in the earthworm Aporrectodea tuberculata (Eisen) were measured to find out their possible induction under Cu and Zn exposure and differences in the responses between two populations with different exposure history. The biomarkers applied were concentration of metallothioneins (MT), and cytochrome P4501A (CYP1A) monooxygenase and glutathione-S-transferase (GST) activities. These were measured from earthworms sampled at three distances from a steel smelter in Finland and from the individuals from two populations, one with and another without earlier metal exposure, exposed to three combined Cu/Zn concentrations in the laboratory. In the field, MT concentration, and cytochrome CYP1…

Cytoplasmfood.ingredientHealth Toxicology and MutagenesisPopulationToxicologymedicine.disease_causefoodbiology.animalMicrosomesmedicineLumbricidaeMetallothioneinAnimalsSoil PollutantsOligochaetaeducationGlutathione Transferaseeducation.field_of_studybiologyEarthwormCopper toxicityGeneral MedicineEnvironmental exposureEnvironmental Exposurebiology.organism_classificationmedicine.diseasePollutionZincSteelEnvironmental chemistryZinc toxicityAporrectodeaMetallothioneinAryl Hydrocarbon HydroxylasesBiomarkersCopperEnvironmental MonitoringEnvironmental pollution (Barking, Essex : 1987)
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Contribution of CYP3A5 to the in vitro hepatic clearance of tacrolimus.

2005

Abstract Background: Tacrolimus is metabolized predominantly to 13-O-demethyltacrolimus in the liver and intestine by cytochrome P450 3A (CYP3A). Patients with high concentrations of CYP3A5, a CYP3A isoenzyme polymorphically produced in these organs, require higher doses of tacrolimus, but the exact mechanism of this association is unknown. Methods: cDNA-expressed CYP3A enzymes and a bank of human liver microsomes with known CYP3A4 and CYP3A5 content were used to investigate the contribution of CYP3A5 to the metabolism of tacrolimus to 13-O-demethyltacrolimus as quantified by liquid chromatography–tandem mass spectrometry. Results: Demethylation of tacrolimus to 13-O-demethyltacrolimus was …

DNA ComplementaryCYP3AClinical BiochemistryPharmacologyBiologyIn Vitro Techniques030226 pharmacology & pharmacyTacrolimus03 medical and health sciences0302 clinical medicinePharmacokineticsCytochrome P-450 Enzyme SystemCytochrome P-450 CYP3AHumansCYP3A7030304 developmental biologyDemethylation0303 health sciencesCYP3A4Biochemistry (medical)MetabolismTacrolimusMicrosomeMicrosomes LiverBaculoviridaeImmunosuppressive AgentsClinical chemistry
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An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.

1996

Abstract We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp 227 -His 428 -Asp 350 in the M. sexta protein) were present, as was the conserved Trp 154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catab…

DNA ComplementaryMolecular Sequence DataBiophysicsSequence HomologyBiologyBiochemistryPolymerase Chain ReactionMiceOpen Reading FramesComplementary DNAMicrosomesCatalytic triadAnimalsHumansAmino Acid SequenceEpoxide hydrolaseMolecular BiologyPeptide sequenceConserved SequenceEpoxide HydrolasesBase SequenceCell BiologyRatsJuvenile HormonesBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesJuvenile hormoneRabbitsOxyanion holeBiochemical and biophysical research communications
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Hepatic metabolism of diclofenac: role of human CYP in the minor oxidative pathways.

1999

The aim of this study was to re-examine the human hepatic metabolism of diclofenac, with special focus on the generation of minor hydroxylated metabolites implicated in the idiosyncratic hepatotoxicity of the drug. Different experimental approaches were used: human hepatocytes, human microsomes, and engineered cells expressing single human CYP (cytochromes P450). Human hepatocytes formed 3'-hydroxy-, 4'-hydroxy-, 5-hydroxy- 4',5-dihydroxy-, and N,5-dihydroxydiclofenac, as well as several lactams. Formation of 4'- and 5-hydroxydiclofenac by human liver microsomes followed a Michaelis-Menten kinetics (Km 9 +/- 1 microM; Vmax 432 +/- 15 pmol/min/mg and Km 43 +/- 5 microM; and Vmax 15.4 +/- 0.6…

DiclofenacMetaboliteIn Vitro TechniquesBiochemistryCell LineHydroxylationCytochrome P-450 CYP2C8chemistry.chemical_compoundTolbutamideCytochrome P-450 Enzyme SystemmedicineHumansBiotransformationCytochrome P-450 CYP2C9PharmacologybiologyAnti-Inflammatory Agents Non-SteroidalCytochrome P450Metabolismmedicine.anatomical_structureBiochemistrychemistrySteroid 16-alpha-HydroxylaseHepatocyteSteroid HydroxylasesMicrosomebiology.proteinMicrosomes LiverAryl Hydrocarbon HydroxylasesOxidation-ReductionDrug metabolismmedicine.drug
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Epoxides derived from various polycyclic hydrocarbons as substrates of homogeneous and microsome-bound epoxide hydratase. A general assay and kinetic…

1976

A general assay for epoxide hydratase using epoxides derived from polycyclic aromatic hydrocarbons as substrates is described. Addition of dimethylsulphoxide to the incubation mixture after incubation allowed unreacted epoxide and its phenolic by-product to be extracted into light petroleum whilst the product dihydrodiol remained in the aqueous phase. The product was then extracted into ethyl acetate and estimated radiochemically. This assay gave low extraction blanks (0.8-3.8%) when six K-region epoxides of polycyclic hydrocarbons were used, with high recoveries of the corresponding dihydrodiol in the ethyl acetate phase (65-89%). Radiochromatograms demonstrated that all the radioactivity …

Epoxide HydrolasesAnthraceneEthyl acetateEpoxideSubstrate (chemistry)PhenanthreneBiochemistryRatschemistry.chemical_compoundKineticsStructure-Activity RelationshipchemistryStyrene oxideMicrosomes LiverPyreneOrganic chemistryAnimalsEpoxy CompoundsPolycyclic HydrocarbonsPolycyclic CompoundsHydro-LyasesEuropean journal of biochemistry
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‘Threshold effect’ of increasing tocopherol ingestion upon the microsomal epoxide hydrolase activity of rat liver

1990

Epoxide HydrolasesMaleChemistryHealth Toxicology and MutagenesisPublic Health Environmental and Occupational HealthAdministration OralRats Inbred StrainsGeneral ChemistryToxicologyRatsMicrosomal epoxide hydrolase activityBiochemistryChemistry (miscellaneous)Rat liverThreshold effectMicrosomes LiverAnimalsVitamin EIngestionTocopherolChromatography High Pressure LiquidFood ScienceFood Additives and Contaminants
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