Search results for "substrate"

showing 10 items of 1018 documents

Nucleoside phosphotransferase in animal tissues. Tissue distribution and kinetic properties

1985

Amphibian, avian and mammal tissues contain a nucleoside phosphotransferase clearly different from those previously described in vegetables and bacteria. Whatever the animal source, the enzyme showed many similar characteristics as far as substrate specificity, dependence upon Mg2+, instability at 37 degrees C, and the protecting effect of nucleotides were concerned. Moreover, when submitted to gel filtration, the enzyme behaved in all cases as a dissociable high molecular weight protein, whose degree of association was controlled by nucleotides. In amphibian and avian tissues multiple forms of the enzyme seem to be present which differ for the substrate concentration at half-maximal veloci…

MaleRanidaeClinical BiochemistryKineticsSize-exclusion chromatographyChick EmbryoBiologySubstrate SpecificityCricetinaeSettore BIO/10 - BiochimicaNucleoside phosphotransferaseIntestine SmallTestisAnimalsNucleotideMagnesiumHorsesMolecular Biologychemistry.chemical_classificationEffectorPhosphotransferasesTemperatureBrainCell BiologyGeneral Medicinebiology.organism_classificationRatsKineticsEnzymeNucleoside phosphotransferaseTissue distributionchemistryBiochemistryChromatography GelCattleRabbitsChickensPhosphotransferasesBacteriaSpleen
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Fat oxidation at rest and during exercise in male monozygotic twins

2019

Abstract Purpose We aimed to investigate if hereditary factors, leisure-time physical activity (LTPA) and metabolic health interact with resting fat oxidation (RFO) and peak fat oxidation (PFO) during ergometer cycling. Methods We recruited 23 male monozygotic twin pairs (aged 32–37 years) and determined their RFO and PFO with indirect calorimetry for 21 and 19 twin pairs and for 43 and 41 twin individuals, respectively. Using physical activity interviews and the Baecke questionnaire, we identified 10 twin pairs as LTPA discordant for the past 3 years. Of the twin pairs, 8 pairs participated in both RFO and PFO measurements, and 2 pairs participated in either of the measurements. We quantif…

MaleSports medicinePhysiologyIntraclass correlationTwinsMonozygotic twinDETERMINANTSlipiditliikuntaglukoosiFats0302 clinical medicineFat oxidationlipid metabolismSUBSTRATE OXIDATIONOrthopedics and Sports MedicineOral glucose tolerance315 Sport and fitness sciencesaineenvaihduntaAdiposityexerciseINSULIN SENSITIVITYhapettuminenArea under the curve1184 Genetics developmental biology physiologytwinsGeneral MedicineVARIABILITYCardiologyOriginal ArticleOxidation-Reductionfyysinen aktiivisuusAdultmedicine.medical_specialtyRest030209 endocrinology & metabolismMotor ActivityDIETARY-FATCAPACITYYoung Adult03 medical and health sciencesTIME PHYSICAL-ACTIVITYPhysiology (medical)Internal medicineCARBOHYDRATEmedicineHumansExerciseOral glucose toleranceMetabolic healthkaksostutkimusbusiness.industryINTENSITYPublic Health Environmental and Occupational HealthCalorimetry IndirectTwins Monozygotic030229 sport sciencesGlucose Tolerance TestConfidence intervalLipid metabolismoral glucose toleranceYOUNGbusiness
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Mass spectrometric identification of the amino donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles.

1991

Four different transglutaminase-modified forms of a protein secreted by the rat seminal vesicles (SV-IV) were synthesized in vitro and characterized. FAB maps of both the native protein and its derivatives, produced by the purified guinea pig liver enzyme in the presence or absence of the polyamine spermidine, were obtained by mass spectrometric analysis after proteolytic digestions. Two differently derivatized SV-IV molecular forms, both possessing only one glutamine residue out of two (Gln-86) cross-linked to endogenous lysine residues, were produced when spermidine was omitted from the reaction mixture: (i) an insoluble homopolymer in which Lys-2, -4, -59, -78, -79, and -80 were involved…

MaleTissue transglutaminaseSeminal Plasma ProteinsLysineGuinea PigsMolecular Sequence DataBiochemistryMass SpectrometrySubstrate SpecificityResidue (chemistry)chemistry.chemical_compoundAnimalsAmino Acid Sequencechemistry.chemical_classificationIsopeptide bondTransglutaminasesbiologyHydrolysisSeminal Plasma ProteinsProstatic Secretory ProteinsProteinsSeminal VesiclesRats Inbred StrainsRatsSpermidineSecretory proteinchemistryBiochemistryLiverbiology.proteinPolyamineChromatography LiquidBiochemistry
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Formation of mono- and diglucuronides and other glycosides of benzo(a)pyrene-3,6-quinol by V79 cell-expressed human phenol UDP-glucuronosyltransferas…

1995

Glucuronidation of quinols of polycyclic aromatic hydrocarbons (PAHs) represents an important detoxication pathway preventing toxic quinone/quinol redox cycles. Therefore, mono- and diglucuronide formation of benzo(a)pyrene-3,6-quinol was investigated and compared to that of structurally related 3,6-dihydroxychrysene and simple phenols (1-naphthol and 4-methylumbelliferone) using V79 cell-expressed human UGT1.6 (= P1) and human UGT1.7 (= P4). Properties of human UGT1.6 were compared to those of the rat ortholog. Cofactors related to UDP-glucuronic acid such as UDP-galacturonic acid and UDP-glucose were also studied. It was found that rat and human UGT1.6 and human UGT1.7 catalyse monoglucur…

MaleUridine Diphosphate GlucoseGlucuronosyltransferaseStereochemistryGlucuronidationGlucuronatesmacromolecular substancesBiochemistryIsozymeSubstrate Specificitychemistry.chemical_compoundGlucosidesAnimalsHumansPhenolsBenzopyrenesGlucuronosyltransferaseRats WistarCarcinogenPharmacologychemistry.chemical_classificationbiologyGlycosideHydroquinonesRatsQuinonechemistryBenzo(a)pyreneBiochemistryUridine Diphosphate Glucuronic Acidbiology.proteinBiochemical Pharmacology
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Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaste…

1991

Dihydropterin oxidase catalyses the oxidation of 7,8-dihydropteridines into their fully oxidized products, and is involved in the biosynthesis of isoxanthopterin. Fifteen Drosophila melanogaster mutants, selected for their low pterin and isoxanthopterin content, were assayed for dihydropterin oxidase activity. The activity was around 100% in most mutants tested, slightly reduced in red, g and dke, and undetectable in lix. In flies carrying various doses of the lix+ allele, a correlation was found between enzyme activity and the number of lix+ copies in the genome. The results suggest that lix is the structural gene for the dihydropterin oxidase enzyme. Isoxanthopterin was quantitated in str…

MaleX ChromosomeGenotypeMutantSubstrate Specificitychemistry.chemical_compoundDihydropterin oxidase activityDrosophilidaeGeneticsAnimalsPterinMolecular BiologyCrosses Geneticchemistry.chemical_classificationbiologyPteridinesStructural geneTemperatureChromosome Mappingbiology.organism_classificationEnzyme assayEnzymeDrosophila melanogasterchemistryBiochemistryMutationbiology.proteinFemaleDrosophila melanogasterOxidoreductasesMoleculargeneral genetics : MGG
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Different deoxyribonucleases in human lymphocytes

1974

Abstract The distribution pattern of deoxyribonuclease activities in human lymphocytes has been examined by micro-disc-electrophoresis. Four groups of deoxyribonuclease activities, differing in their electrophoretic mobility, in the nature of their optimal substrate and in their optimal incubation conditions, are characterized. There are two alkaline DNase-activities. One corresponds to DNase I (EC 3.1.4.5), the other having pH optimum of about pH 9.0, prefers denatured DNA as substrate and is not dependent on divalent cations. The fractions with an acid pH optimum can be subdivided into two groups, which differ in their activity towards native DNA, towards denatured DNA, in their activity …

Malechemistry.chemical_classificationDeoxyribonucleasesHot TemperatureSubstrate (chemistry)DeoxyribonucleaseHydrogen-Ion ConcentrationIn Vitro TechniquesBiologyDivalentElectrophoresischemistry.chemical_compoundchemistryBiochemistryGeneticsHumansElectrophoresis Polyacrylamide GelLymphocytesDeoxyribonuclease IDeoxyribonucleasesIncubationDNANucleic Acids Research
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Interrelationship between demethylation of p-nitroanisole and conjugation of p-nitrophenol in rat liver

1973

The metabolism of p-nitroanisole (pNA) and p-nitrophenol (pNP) was studied in isolated rat livers perfused with a hemoglobin-free medium. The activity and viability of the surviving organ was tested by recording pH, “arterial” and “venous” oxygen tension as well as the disappearance of added pNP. pNA is converted to its primary metabolite pNP which, in turn, is excreted into the perfusion medium as conjugates. The coordination of pNA oxidation and the conjugation reactions of pNP were investigated. When 50 μM pNA is added as substrate 0.4±0.1 nmoles×ml−1×(g liver)−1 are excreted as pNP-glucuronide and 3.5±0.2 nmoles×ml−1×(g liver)−1 as the sulphate within 90 min. When pNP itself (50 μM) is …

Maleinorganic chemicalsGlucuronidationGlucuronatesAnisolesIn Vitro TechniquesMethylationNitrophenolsOrganophosphorus CompoundsSulfationAnimalsheterocyclic compoundsGlucuronosyltransferaseGlucuronidaseDemethylationPharmacologyChromatographyChemistryHydrolysisLiver cellSubstrate (chemistry)General MedicineMetabolismHydrogen-Ion ConcentrationNitro CompoundsRatsOxygen tensionOxygenenzymes and coenzymes (carbohydrates)LiverBiochemistryMicrosomes LiverSulfatasesGlucuronideOxidation-ReductionGlucosidasesNaunyn-Schmiedeberg's Archives of Pharmacology
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The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates

1995

The present study examined the distribution of the pro-hormone convertases PC1, PC2, furin, PACE4 and PC5 in the rat heart. Northern blot analysis of RNA extracted from cardiac tissues showed high levels of furin and PACE4 mRNA in the atria and ventricles, while PC5 mRNA was found to be expressed at high levels in the dorsal aorta. Although undetectable by Northern blot analysis, both PC1 and PC2 mRNA were detected by in situ hybridization and immunohistochemistry in discrete regions of the intracardiac para-aortic ganglia. In situ hybridization studies also showed that furin mRNA was observed in all cardiac tissues and cells, consistent with the previously reported ubiquitous expression of…

Malemedicine.medical_specialtyHistologyMolecular Sequence DataGene ExpressionIn situ hybridizationSubstrate SpecificityPathology and Forensic MedicineRats Sprague-DawleyDorsal aortaInternal medicineGene expressionmedicineAnimalsAspartic Acid EndopeptidasesAmino Acid SequenceNorthern blotFurinIn Situ HybridizationMessenger RNAbiologyMyocardiumSerine EndopeptidasesRNACell BiologyBlotting NorthernImmunohistochemistryMolecular biologyHormonesRatsEndocrinologycardiovascular systembiology.proteinImmunohistochemistryCell and Tissue Research
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The anaerobic metabolism of malate of Saccharomyces bailii and the partial purification and characterization of malic enzyme.

1982

1. The main pathway of the anaerobic metabolism of l-malate in Saccharomyces bailii is catalyzed by a l-malic enzyme. 2. The enzyme was purified more than 300-fold. During the purification procedure fumarase and pyruvate decarboxylase were removed completely, and malate dehydrogenase and oxalacetate decarboxylase were removed to a very large extent. 3. Manganese ions are not required for the reaction of malic enzyme of Saccharomyces bailii, but the activity of the enzyme is increased by manganese. 4. The reaction of l-malic enzyme proceeds with the coenzymes NAD and (to a lesser extent) NADP. 5. The Km-values of the malic enzyme of Saccharomyces bailii were 10 mM for l-malate and 0.1 mM for…

Malic enzymeMalatesSaccharomyces cerevisiaeBiochemistryMicrobiologyMalate dehydrogenasechemistry.chemical_compoundSaccharomycesSpecies SpecificityMalate DehydrogenaseGeneticsAnaerobiosisMolecular Biologychemistry.chemical_classificationfungifood and beveragesSubstrate (chemistry)General MedicineKineticsEnzymechemistryBiochemistryFumaraseMalic acidNAD+ kinasePyruvate decarboxylaseArchives of microbiology
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Photoinduced mass transport in amorphous As‐S‐Se films

2012

Direct surface patterning due to photoinduced mass transport in amorphous As-S-Se films has been studied. Illumination of the films with two orthogonally (±45°) polarized beam interference pattern causes the formation of surface relief gratings on the films due to lateral mass transport regarding to light propagation direction. The obtained experimental results showed the dependence of photoinduced surface relief depth (Δh) on film thickness during holographic recording from film side as well as from glass substrate side. After constant exposure doses for the films with a thickness d 1 μm values of Δh do not depend significantly on the film thickness for recording from film side but decreas…

Mass transportMaterials scienceSurface reliefbusiness.industryLateral massSubstrate (electronics)Condensed Matter PhysicsAmorphous solidOpticsOptoelectronicsbusinessSurface relief gratingHolographic recordingBeam (structure)physica status solidi c
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