Search results for "substrate"

showing 10 items of 1018 documents

Measurement of substrate-induced oxygen uptake during microsomal drug oxidation using a gold micro-electrode.

1975

1. A resin-coated gold micro-electrode has been used for polarographic determination of oxygen concentration in liver microsomal suspensions from phenobarbital-pretreated rats. 2. The rate of oxygen uptake on addition of an NADPH-regenerating system and the rate after addition of various substrates of the mixed function oxidase system were measured. The rate of oxygen uptake was faster in the presence of substrate than in the presence of NADPH alone. 3. Kinetic constants (Km and V max) for biphenyl, hexobarbital, ethylmorphine, naphthalene and SKF 525-A measured by this technique compare favourably with those obtained either by measurements of NADPH oxidation, or chemical measurements of su…

MaleHealth Toxicology and MutagenesisInorganic chemistryHexobarbitalNaphthalenesToxicologyBiochemistryOxygen ConsumptionmedicineAnimalsPharmacologyPolarographyMorphine DerivativesCell-Free SystemMorphineChemistryProadifenBiphenyl CompoundsSubstrate (chemistry)General MedicineNADPH oxidationEthylmorphineRatsKineticsHexobarbitalMixed Function OxidaseMicrosomes LiverLimiting oxygen concentrationGoldOxidoreductasesMicroelectrodesOxidation-ReductionDrug metabolismNADPmedicine.drugPolarographyXenobiotica; the fate of foreign compounds in biological systems
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Evaluation of an automated chromogenic substrate assay for the rapid determination of hirudin in plasma.

1995

Abstract A fully mechanized chromogenic substrate assay method for the rapid and specific determination of recombinant hirudin (r-hirudin) in citrated plasma on clinical chemistry analyzers (Hitachi 911 and Cobas Mira) is described. In a first step, 12 μl sample volume is mixed with the chromogenic substrate. Due to the almost immediate action of hirudin the inhibitory reaction and the cleavage of the substrate is started simultaneously when bovine thrombin is added in excess. This excludes interferences by antithrombin III or heparin cofactor II. The change in absorbance/min is recorded at 405 nm. The measuring range is about 0.2 – 4.0 mg/l r-hirudin on both analyzers. Precision is charact…

MaleHirudinEnzyme-Linked Immunosorbent AssayAbsorbanceAutomationReference ValuesBlood plasmamedicineAnimalsHumansHeparin cofactor IIChromatographyChemistryChromogenicAntithrombinThrombinSubstrate (chemistry)Chromogenic substrate assayHematologyHirudinsMiddle AgedRecombinant ProteinsChromogenic CompoundsCalibrationCattleColorimetryFemalePartial Thromboplastin TimeOligopeptidesmedicine.drugThrombosis research
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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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1-imidazolyl(alkyl)-substituted di- and tetrahydroquinolines and analogues: syntheses and evaluation of dual inhibitors of thromboxane A(2) synthase …

2000

A series of 1-imidazolyl(alkyl)-substituted quinoline, isoquinoline, naphthalene, benzo[b]furan, and benzo[b]thiophene derivatives was synthesized as dual inhibitors of thromboxane A(2) synthase (P450 TxA(2)) and aromatase (P450 arom). Dual inhibition of these enzymes could be a novel strategy for the treatment of mammary tumors and the prophylaxis of metastases. The most potent dual inhibitors, 5-(2-imidazol-1-ylethyl)-7,8-dihydroquinoline (31) (P450 TxA(2): IC(50) = 0.29 microM; P450 arom: IC(50) = 0.50 microM) and its 5, 6-saturated analogue 30 (P450 TxA(2): IC(50) = 0.68 microM; P450 arom: IC(50) = 0.38 microM), showed a stronger inhibition of both target enzymes than the reference comp…

MaleMagnetic Resonance SpectroscopyThromboxaneStereochemistryIn Vitro TechniquesSubstrate SpecificityRats Sprague-DawleyThromboxane A2chemistry.chemical_compoundLipoxygenaseThromboxane A2MicrosomesDrug DiscoveryAnimalsHumansDazoxibenIsoquinolineEnzyme InhibitorsbiologyAromatase InhibitorsImidazolesRatsThromboxane B2Thromboxane B2chemistrybiology.proteinQuinolinesMolecular MedicineSpectrophotometry UltravioletThromboxane-A synthaseCyclooxygenaseThromboxane-A SynthaseJournal of medicinal chemistry
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Distant Homology Modeling of LCAT and Its Validation through In Silico Targeting and In Vitro and In Vivo Assays

2013

LCAT (lecithin:cholesterol acyltransferase) catalyzes the transacylation of a fatty acid of lecithin to cholesterol, generating a cholesteryl ester and lysolecithin. The knowledge of LCAT atomic structure and the identification of the amino acids relevant in controlling its structure and function are expected to be very helpful to understand the enzyme catalytic mechanism, as involved in HDL cholesterol metabolism. However - after an early report in the late '90 s - no recent advance has been made about LCAT three-dimensional structure. In this paper, we propose an LCAT atomistic model, built following the most up-to-date molecular modeling approaches, and exploiting newly solved crystallog…

MaleModels MolecularProtein StructureDrug Research and DevelopmentProtein Conformationlcsh:MedicineBiologyBiochemistryCatalysisSubstrate SpecificityPhosphatidylcholine-Sterol O-AcyltransferaseMicechemistry.chemical_compoundEnzyme activatorTransacylationProtein structureDrug DiscoveryHydrolaseCatalytic triadBiochemical SimulationsMedicine and Health SciencesAnimalsHumansHomology modelingBiomacromolecule-Ligand Interactionslcsh:SciencePharmacologyBinding SitesPlasma ProteinsMultidisciplinarylcsh:RBiology and Life SciencesProteinsEnzyme structureEnzyme ActivationMolecular Docking SimulationchemistryBiochemistryMutationEnzyme StructureEnzymologyBiocatalysisCholesteryl esterlcsh:QResearch ArticleBiotechnologyPLoS ONE
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Differential modulation of CYP2E1 activity by cAMP-dependent protein kinase upon Ser129 replacement.

1998

Many toxic compounds are activated by cytochrome P450 (CYP) 2E1 to reactive metabolites, which represents a potential hazard for cellular homeostasis. Therefore knowledge about CYP2E1 regulation could be of great biological importance. It has been shown that CYP2E1 is controlled transcriptionally and post-translationally by phosphorylation. In the present study we investigated the role of serine-129 (Ser129) in the protein kinase A (PKA) recognition sequence motif Arg-Arg-Phe-Ser129. To gain further insights into the possible relevance of Ser129 for CYP2E1 function, Ser129 was replaced by alanine (Ala) or glycine (Gly) by site-directed mutations of the cDNA coding for CYP2E1. The mutant cDN…

MaleMutantCellular homeostasisTransfectionDimethylnitrosamineSubstrate SpecificityRats Sprague-DawleyMiceCricetulusCricetinaeIsoniazidSerineAnimalsEnzyme inducerPhosphorylationProtein kinase ALungCells Culturedchemistry.chemical_classificationMice Inbred BALB CbiologyCytochrome P-450 CYP2E1Cell BiologyFibroblastsMolecular biologyCyclic AMP-Dependent Protein KinasesAmino acidRatsEnzymechemistryBiochemistryAmino Acid SubstitutionBucladesineEnzyme InductionInactivation MetabolicMutationbiology.proteinMicrosomes LiverPhosphorylationDemethylaseMutagensExperimental cell research
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Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases.

1992

1. Dihydrodiol dehydrogenase activities were investigated in rabbit liver. Using a five-step purification scheme, eight isoenzymes of dihydrodiol dehydrogenase with isoelectric points of 5.55-9.3 and promoter molecular masses of 34-35 kDa were purified to apparent homogeneity and designated CF-1 to CF-6, CM-1 and CM-2. 2. CF-1 and CF-2 had near-neutral isoelectric points of 7.4 and 6.8 and molecular masses of about 125 kDa in the native state. Both enzymes readily accepted NAD+ as well as NADP+ as coenzymes, had relatively low Km values of 0.33 mM and 0.47 mM for benzene dihydrodiol and resembled previously described carbonyl reductases in their substrate specificity towards ketones and qui…

MaleOxidoreductases Acting on CH-CH Group DonorsCarbonyl ReductaseStereochemistryAldo-Keto ReductasesDehydrogenaseReductaseBiochemistryCofactorCatalysisSubstrate SpecificityAldehyde Reductasepolycyclic compoundsAnimalsTissue DistributionIsoelectric PointAldehyde ReductaseAldo-keto reductasebiologyChemistryHydroxysteroid DehydrogenasesAntibodies MonoclonalHydroxysteroid DehydrogenasesIsoenzymesMolecular WeightAlcohol OxidoreductasesBiochemistryLiverbiology.proteinElectrophoresis Polyacrylamide GelNAD+ kinaseRabbitsOxidoreductasesEuropean journal of biochemistry
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The Insulin Receptor Substrate 1 (Irs1) in Intestinal Epithelial Differentiation and in Colorectal Cancer

2012

Colorectal cancer (CRC) is associated with lifestyle factors that affect insulin/IGF signaling, of which the insulin receptor substrate 1 (IRS1) is a key transducer. We investigated expression, localization and pathologic correlations of IRS1 in cancer-uninvolved colonic epithelium, primary CRCs with paired liver metastases and in vitro polarizing Caco2 and HT29 cells. IRS1 mRNA and protein resulted higher, relative to paired mucosa, in adenomas of familial adenomatous polyposis patients and in CRCs that overexpressed c-MYC, ß-catenin, InsRß, and IGF1R. Analysis of IRS1 immunostaining in 24 cases of primary CRC with paired colonic epithelium and hepatic metastasis showed that staining inten…

MalePathologyAnatomy and PhysiologySettore MED/06 - Oncologia MedicaMetastasisIntestinal mucosaInsulin Signaling CascadeMolecular Cell BiologyGastrointestinal CancersBasic Cancer ResearchInsulinIntestinal MucosaInsulin-like Growth FactorCOLON-CARCINOMA-CELLS; GROWTH-FACTOR RECEPTOR; BETA-CATENIN; FACTOR-I; IGF-I; NUCLEAR TRANSLOCATION; ADENOMATOUS POLYPOSIS; STEM-CELL; EXPRESSION; MUTATIONSMultidisciplinarybiologyChemistryQLiver NeoplasmsRCell PolarityCell DifferentiationSignaling CascadesGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structureOncologyMedicineFemaleColorectal NeoplasmsHT29 CellsResearch ArticleSignal TransductionAdultendocrine systemmedicine.medical_specialtyColonScienceIRS1 IGF1R colorectal cancerEndocrine SystemGastroenterology and HepatologySignaling PathwaysFamilial adenomatous polyposisHT29 CellsmedicineHumansBiologyAgedInsulin-like growth factor 1 receptorEndocrine Physiologymedicine.diseasedigestive system diseasesEpitheliumIRS1Insulin receptorInsulin Receptor Substrate Proteinsbiology.proteinCancer researchCaco-2 CellsImmunostainingInsulin-Dependent Signal Transduction
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Association of a polyuridylate-specific endoribonuclease with small nuclear ribonucleo-proteins which had been isolated by affinity chromatography us…

1983

Immunoglobulins, containing antibodies against U1-snRNP, have been prepared from a patient with systemic lupus erythematosus. After coupling these antibodies to a Sepharose matrix, U-snRNPs have been isolated and purified from rat liver nuclei by use of immunoaffinity chromatography. The resulting RNPs had the typical protein pattern of U-sn RNPs and a sedimentation coefficient of 12 S. The U-snRNP preparation was associated with an endoribonuclease which required Mg2+ for optimal activity. The enzyme, with an pH optimum of 6.2, degraded only poly(U). Other single-stranded polyribo- and polydeoxyribonucleotides, tRNA, as well as double-stranded RNA and DNA were not digested. The products of…

MalePoly UEndoribonucleaseAntibody AffinityBiologyenvironment and public healthBiochemistryChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyEndoribonucleasesAnimalsHumansLupus Erythematosus Systemicchemistry.chemical_classificationImmunochemistryRNARats Inbred StrainsRibonucleoproteins Small NuclearMolecular biologyRatsEnzymechemistryLiverRibonucleoproteinsAntibodies AntinuclearImmunoglobulin GRNA splicingTransfer RNADNAEuropean journal of biochemistry
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The major isozyme of rat cardiac glutathione transferases. Its correspondence to hepatic transferase X.

1986

1. A major isozyme of rat heart glutathione transferase was purified to homogeneity by Sephadex G-200 gel filtration, ammonium sulfate precipitation, CM-cellulose chromatography and affinity chromatography on S-hexylglutathione-linked Sepharose 6B. 2. The purified isozyme was a dimer with an apparent relative molecular mass of 50000 composed of two Yb-size subunits (Mr= 26 500). The isozyme is immunologically related to rat liver glutathione transferase X and 3–3, especially closely to transferase X, and no immunological cross-reactivity with subunits 1 and 2 of hepatic glutathione transferases was observed. The isoelectric point (pI = 6.9) of the isozyme was identical with and the substrat…

MalePyruvate dehydrogenase lipoamide kinase isozyme 1ImmunodiffusionBiologyBiochemistryIsozymeChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyTransferaseAnimalsIsoelectric PointGlutathione TransferaseMolecular massMyocardiumRats Inbred StrainsGlutathioneHydrogen-Ion ConcentrationMolecular biologyRatsIsoenzymesMolecular WeightIsoelectric pointchemistryBiochemistryLiverChromatography GelElectrophoresis Polyacrylamide GelEuropean journal of biochemistry
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