Search results for "kinetics"

showing 10 items of 2224 documents

Pigment organization and energy transfer dynamics in isolated photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, P…

2002

Abstract Green plant photosystem I (PSI) consists of at least 18 different protein subunits. The roles of some of these protein subunits are not well known, in particular those that do not occur in the well characterized PSI complexes from cyanobacteria. We investigated the spectroscopic properties and excited-state dynamics of isolated PSI-200 particles from wild-type and mutant Arabidopsis thaliana plants devoid of the PSI-G, PSI-K, PSI-L, or PSI-N subunit. Pigment analysis and a comparison of the 5K absorption spectra of the various particles suggests that the PSI-L and PSI-H subunits together bind approximately five chlorophyll a molecules with absorption maxima near 688 and 667nm, that…

Time FactorsAbsorption spectroscopyProtein subunitPhotosynthetic Reaction Center Complex ProteinsArabidopsisLight-Harvesting Protein ComplexesBiophysicsBiologyPhotosystem Ichemistry.chemical_compoundPhase (matter)MoleculePlant ProteinsQuantitative Biology::BiomoleculesPhotosystem I Protein ComplexTemperaturePigments Biologicalbeta CaroteneFluorescenceKineticsCrystallographySpectrometry FluorescenceEnergy TransferchemistryChlorophyllThermodynamicsHigh Energy Physics::ExperimentAbsorption (chemistry)Research Article
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Ferricytochrome c encapsulated in silica hydrogels: correlation between active site dynamics and solvent structure.

2003

Ferricytochrome c encapsulated in silica hydrogels has been prepared by the sol-gel technique following, with some modifications, the procedure originally developed by Ellerby et al. (Science 255 1113 (1992)). A suitable preparation of hydrogels enables having both 'wet' and 'dry' samples. Wet samples have a high water content: as the temperature is lowered below approximately 260 K, water freezes and the samples crack. On the contrary, dry samples have a low water content (hydration h approximately equal 0.35): in these conditions water does not freeze even at cryogenic temperatures and the samples remain transparent and non-cracking. The dynamics of ferricytochrome c and its dependence on…

Time FactorsAbsorption spectroscopySilicon dioxideDrug CompoundingAnalytical chemistryBiophysicsSilica GelCapsulesCytochrome c GroupSpectrum Analysis RamanBiochemistrychemistry.chemical_compoundDrug StabilityFreezingAnimalsHorsesWater contentBinding SitesbiologySilica gelSpectrum AnalysisOrganic ChemistryTemperatureActive siteWaterHydrogelsAtmospheric temperature rangeSilicon DioxideSolventKineticschemistrySelf-healing hydrogelsbiology.proteinSolventsBiophysical chemistry
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Oxygen uptake kinetics and energy system's contribution around maximal lactate steady state swimming intensity

2017

Made available in DSpace on 2018-11-26T17:20:55Z (GMT). No. of bitstreams: 0 Previous issue date: 2017-02-28 Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Ministry of Education of Brazil The purpose of this study was to examine the oxygen uptake ((V) over dotO(2)) kinetics and the energy systems' contribution at 97.5, 100 and 102.5% of the maximal lactate steady state (MLSS) swimming intensity. Ten elite female swimmers performed three-to-five 30 min submaximal constant swimming bouts at imposed paces for the determination of the swimming velocity (v) at 100% MLSS based on a 7 x 200 m intermittent incremental protocol until voluntary exhaustion to find the v associated…

Time FactorsAnaerobic ThresholdPhysiologyVelocitylcsh:MedicinePathology and Laboratory MedicineOxygenBiochemistryOxygen uptake kinetics0302 clinical medicineMedicine and Health SciencesPublic and Occupational Healthlcsh:ScienceFatigueMultidisciplinaryChemistryPhysicsTime constantClassical Mechanics16. Peace & justiceSports ScienceBody FluidsChemistryvVO2maxBloodPhysical SciencesLactatesFemaleAnatomyAnaerobic exerciseResearch ArticleChemical ElementsSportsAdolescentchemistry.chemical_elementBioenergetics03 medical and health sciencesYoung AdultMotionAnimal scienceOxygen ConsumptionSigns and SymptomsDiagnostic MedicineHumansLactic AcidSports and Exercise MedicineEnergy systemExerciseSwimmingBehaviorBiological Locomotionlcsh:RBiology and Life Sciences030229 sport sciencesPhysical ActivityIntensity (physics)OxygenKineticsAthletesPhysical FitnessExercise TestPhysical EnduranceRecreationlcsh:QSteady state (chemistry)Energy Metabolism030217 neurology & neurosurgery
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Secretion of neutral and acid DNases in cultivated human lymphocytes after incubation with DNA; possible consequences for inhalation anesthesia.

1995

Abstract After incubation with DNA human lymphocytes release neutral and acid DNase activities into the culture medium; the release depends on DNA concentration and time of cultivation. The electrophoretic mobility of the released neutral DNase activity is in accordance with DNase I and the electrophoretic mobility of the released acid DNase activity with DNase II. The released DNase activities do not originate from dead cells and are not influenced by blast cell formation. The anesthetic halothane can inhibit the released neutral and acid DNase activities. Inhalation anesthesia can possibly disturb the correlation between DNA and DNases in human blood.

Time FactorsBiologyGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundPrecursor cellmedicineDeoxyribonuclease IHumansSecretionLymphocytesIncubationCells CulturedDeoxyribonucleasesEndodeoxyribonucleasesInhalationDose-Response Relationship DrugDNAHydrogen-Ion ConcentrationDose–response relationshipKineticschemistryBiochemistryAnestheticHalothaneAnesthesia InhalationHalothaneDNAmedicine.drugZeitschrift fur Naturforschung. C, Journal of biosciences
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Detoxifying antitumoral drugs via nanoconjugation: the case of gold nanoparticles and cisplatin

2021

Nanoparticles (NPs) have emerged as a potential tool to improve cancer treatment. Among the proposed uses in imaging and therapy, their use as a drug delivery scaffold has been extensively highlighted. However, there are still some controversial points which need a deeper understanding before clinical application can occur. Here the use of gold nanoparticles (AuNPs) to detoxify the antitumoral agent cisplatin, linked to a nanoparticle via a pH-sensitive coordination bond for endosomal release, is presented. The NP conjugate design has important effects on pharmacokinetics, conjugate evolution and biodistribution and results in an absence of observed toxicity. Besides, AuNPs present unique o…

Time FactorsCancer TreatmentMetal Nanoparticleslcsh:MedicinePharmacologyMiceNanotechnologyTissue Distributionlcsh:Sciencemedia_commonDrug DistributionDrug CarriersMultidisciplinaryChemistryDNA NeoplasmOrgan SizeHydrogen-Ion ConcentrationEndocytosisOncologyColloidal goldDrug deliveryInactivation MetabolicMedicinemedicine.drugResearch ArticleBiotechnologyDrugBiodistributionDrugs and Devicesmedia_common.quotation_subjectMaterials ScienceAntineoplastic AgentsMaterial by AttributePharmacokineticsCell Line TumormedicineAnimalsHumansPharmacokineticsBiologyNanomaterialsCisplatinUnited States Food and Drug Administrationlcsh:RChemotherapy and Drug TreatmentUnited StatesBionanotechnologylcsh:QGoldNanocarriersCisplatinConjugate
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Fluctuation Methods To Study Protein Aggregation in Live Cells: Concanavalin A Oligomers Formation

2011

Prefibrillar oligomers of proteins are suspected to be the primary pathogenic agents in several neurodegenerative diseases. A key approach for elucidating the pathogenic mechanisms is to probe the existence of oligomers directly in living cells. In this work, we were able to monitor the process of aggregation of Concanavalin A in live cells. We used number and brightness analysis, two-color cross number and brightness analysis, and Raster image correlation spectroscopy to obtain the number of molecules, aggregation state, and diffusion coefficient as a function of time and cell location. We observed that binding of Concanavalin A to the membrane and the formation of small aggregates paralle…

Time FactorsCell SurvivalCellSpectroscopy Imaging and Other TechniquesBiophysicsProtein aggregationCell morphologyCell membraneDiffusion03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineProtein structure2-NaphthylaminemedicineConcanavalin AAnimalsconfocal microscopy super resolution protein aggregation kinetics in live cells amyloid related pathologiesAnnexin A5Protein Structure QuaternaryCell Shape030304 developmental biology0303 health sciencesbiologySpectrum AnalysisCell MembraneFibroblastsEmbryo MammalianCell biologyMembranemedicine.anatomical_structurechemistryConcanavalin Abiology.proteinLaurdan030217 neurology & neurosurgeryFluorescein-5-isothiocyanateLaurates
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Alterations of Activities of Ribonucleases and Polyadenylate Polymerase in Synchronized Mouse L Cells

1977

The activities of the three known catabolic and the one anabolic polyadenylate enzymes have been determined in synchronized L5178y cells: endoribonuclease, exoribonuclease, 5'-nucleotidase and poly(A) polymerase (Mg2+-dependent). These four enzymes were found primarily in the nuclear fraction. The activity of poly(A) polymerase remains essentially constant during the transition from G1 to S phase. However, the poly(A) catabolic enzyme activities increase parallel with DNA synthesis; the endoribonuclease activity increases 4-fold during G1 to S phase, the exoribonuclease and the nucleotidase activities increasing 30-fold and 16-fold. During the S phase the poly(A)-degrading enzymes are far m…

Time FactorsEndoribonuclease activityEndoribonucleaseMitosisBiochemistryCell LineStructure-Activity RelationshipL CellsRibonucleasesExoribonucleaseNucleotidasePolyadenylatePolymerasechemistry.chemical_classificationbiologyDNA synthesisPolynucleotide AdenylyltransferaseNucleotidyltransferasesMolecular biologyMolecular WeightKineticsEnzymeBiochemistrychemistrybiology.proteinCell DivisionEuropean Journal of Biochemistry
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Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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Cerebral toxicity of penicillins in relation to their hydrophobic character

1975

The neurotoxic effects of ticarcillin, methicillin, phenthicillin, oxacillin, cloxacillin and dicloxacillin were studied in the conscious rabbit. During and after intravenous administration of 1.2 and 2.4 g/kg, resp., over 50 min the blood concentrations of the drugs were determined and the neurotoxicity assessed by continuous recording of the electroencephalogram. The hydrophobia of the penicillins was characterized by determination of their partition coefficients between isobutanol and buffer solution pH 7.4. The penicillins showed quite different neurotoxic properties. A close correlation (r = 0.928) was found between the neurotoxic potency of the penicillins and their partition coeffici…

Time FactorsHydrophobiaPenicillinsPharmacologyDicloxacillinMethicillinStructure-Activity RelationshipCloxacillinpolycyclic compoundsmedicineAnimalsTicarcillinPotencyDicloxacillinInfusions ParenteralcvgOxacillinPharmacologyChromatographyChemistrycvg.computer_videogameNeurotoxicityBrainElectroencephalographyGeneral Medicinebiochemical phenomena metabolism and nutritionmedicine.diseasePartition coefficientPenicillinKineticsTicarcillinPenicillin VFemaleRabbitsCloxacillinmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Equilibrium coverage fluctuations: a new approach to quantify reversible adsorption of proteins.

2005

Time FactorsProtein ConformationKineticsBiophysicsBiosensing TechniquesModels BiologicalAdsorptionAb initio quantum chemistry methodsComputational chemistryElectrochemistryComputer SimulationPhysical and Theoretical ChemistryChemistryReversible adsorptionChemistry PhysicalProteinsSurface Plasmon ResonanceAtomic and Molecular Physics and OpticsNanostructuresKineticsSpectrophotometryAdsorptionStress MechanicalPeptidesMonte Carlo MethodAlgorithmsProtein BindingChemphyschem : a European journal of chemical physics and physical chemistry
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