Search results for "Electrophoresi"

showing 10 items of 1009 documents

Inhibition of B2 receptor internalization delays its dephosphorylation

1997

SucroseReceptor Bradykinin B2Immunoprecipitationmedia_common.quotation_subjectBradykininBradykininCell LineDephosphorylationRadioligand Assaychemistry.chemical_compoundOkadaic AcidConcanavalin APhosphoprotein PhosphatasesHumansEnzyme InhibitorsPhosphorylationInternalizationOxazolesBradykinin Receptor AntagonistsSkinmedia_commonPharmacologyChemistryReceptors BradykininOkadaic acidFibroblastsPrecipitinPrecipitin TestsRadioligand AssayBiochemistryCantharidinIrritantsAutoradiographyPhosphorylationElectrophoresis Polyacrylamide GelMarine ToxinsImmunopharmacology
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Studies on sea urchin oocytes. II. Synthesis of RNA during oogenesis.

1972

Abstract Isolated oocytes of the sea urchin Paracentrotus lividus actively incorporate 3H-uridine into RNA. Labeled RNA was analysed by sucrose gradient and acrylamide gel electrophoresis following cell fractionation. Much of the radioactivity is incorporated at the nucleolar level in the form of rRNA precursors. The kinetics of maturation of these latter suggests that this occurs at a slower rate than during embryogenesis. Other non-nucleolar RNA classes are also actively labelled and retained in the nucleus for many hours. These results are confirmed by an autoradiographic investigation.

SucroseTime FactorsBiologyCell FractionationTritiumOogenesisParacentrotus lividusbiology.animalBotanyCentrifugation Density GradientAnimalsPolyacrylamide gel electrophoresisSea urchinUridineOvumCell NucleusHistocytochemistryEmbryogenesisRNACell BiologyRibosomal RNAbiology.organism_classificationElectrophoresis DiscMolecular WeightBiochemistryRNA RibosomalSea UrchinsAutoradiographyRNAFemaleCell fractionationCell NucleolusExperimental cell research
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Echovirus 1 Endocytosis into Caveosomes Requires Lipid Rafts, Dynamin II, and Signaling EventsV⃞

2004

Binding of echovirus 1 (EV1, a nonenveloped RNA virus) to the α2β1 integrin on the cell surface is followed by endocytic internalization of the virus together with the receptor. Here, video-enhanced live microscopy revealed the rapid uptake of fluorescently labeled EV1 into mobile, intracellular structures, positive for green fluorescent protein-tagged caveolin-1. Partial colocalization of EV1 with SV40 (SV40) and cholera toxin, known to traffic via caveosomes, demonstrated that the vesicles were caveosomes. The initiation of EV1 infection was dependent on dynamin II, cholesterol, and protein phosphorylation events. Brefeldin A, a drug that prevents SV40 transport, blocked the EV1 infection…

SucroseTime FactorsvirusesEndocytic cycleDynamin IIchemistry.chemical_compoundDynamin IIPhosphorylationInternalizationCytoskeletonIn Situ HybridizationIn Situ Hybridization Fluorescencemedia_commonGenes Dominant0303 health sciencesMicroscopy Videobiology030302 biochemistry & molecular biologyArticlesBrefeldin AEndocytosisCell biologyEnterovirus B HumanCholesterolRNA ViralElectrophoresis Polyacrylamide GelProtein BindingSignal TransductionCholera Toxinmedia_common.quotation_subjectIntegrinGreen Fluorescent ProteinsImmunoblottingEndocytosisTransfectionCell Line03 medical and health sciencesCapsidMembrane MicrodomainsViral entryCentrifugation Density GradientAnimalsMolecular Biology030304 developmental biologyBinding SitesBrefeldin ACell MembraneCell BiologyKineticschemistryViral replicationMicroscopy Fluorescencebiology.protein
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Experimental and theoretical evidence of overcharging of calcium silicate hydrate

2007

International audience; Electrokinetic measurements such as electrophoresis may show an inversion of the effective surface charge of colloidal particle called overcharging. This phenomenon has been studied by various theoretical approaches but up to now very few attempts of confrontation between theory and experiment have been conducted. In this work we report electrophoretic measurements as well as Monte Carlo simulations of the electrokinetic potential for the surface of calcium silicate hydrate (Csingle bondSsingle bondH), which is the major constituent of hydrated cement. In the simulations, the surface charge of Csingle bondSsingle bondH nanoparticles in equilibrium with the ionic solu…

Surface PropertiesAnalytical chemistry02 engineering and technology010402 general chemistry01 natural sciencesBiomaterialsElectrokinetic phenomenachemistry.chemical_compoundColloid and Surface ChemistryZeta potentialElectrochemistrySurface chargeColloidsCalcium silicate hydrateParticle SizeMonte Carlo simulationRange (particle radiation)Physics::Biological PhysicsQuantitative Biology::BiomoleculesCalcium silicate hydrateSilicatesWaterZeta potentialCalcium Compounds021001 nanoscience & nanotechnologyElectrostatics0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic Materials[ PHYS.PHYS.PHYS-CHEM-PH ] Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]ElectrophoresisKineticschemistryModels ChemicalChemical physicsSurface charge titrationOverchargingCalcium silicateNanoparticles[PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph]0210 nano-technologyMonte Carlo Method
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Mapping and expression pattern analysis of key components of the major histocompatibility complex class I antigen processing and presentation pathway…

2001

Renal cell carcinoma (RCC) represent approximately 5% of all cancer deaths. At the time of presentation, over 50% of the patients have already developed locally advanced or metastatic disease with five-year survival rates of less than 20%. Although relative resistant to conventional regimens, RCC are partially susceptible to T cell-based immunotherapy. To further develop this treatment modality, two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) was applied for both the mapping of the key components of the major histocompatibility complex (MHC) class I antigen processing and presentation machinery (APM) and the characterization of the constitutive and cytokine-regulated protein e…

T cellClinical BiochemistryAntigen presentationBiologyProteomicsMajor histocompatibility complexPeptide MappingBiochemistryAnalytical ChemistryWestern blotInterferonTumor Cells CulturedmedicineHumansElectrophoresis Gel Two-DimensionalCarcinoma Renal CellAntigen PresentationTwo-dimensional gel electrophoresismedicine.diagnostic_testHistocompatibility Antigens Class IMolecular biologyKidney Neoplasmsmedicine.anatomical_structurebiology.proteinAntibodymedicine.drugELECTROPHORESIS
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Alteration of DNA topoisomerase II activity during infection of H9 cells by human immunodeficiency virus type 1 in vitro: a target for potential ther…

1990

Infection of H9 cells with human immunodeficiency virus type 1 (HIV-1) was found to decrease the phosphorylation of DNA topoisomerase II during the initial phase of infection. Simultaneously, with a later overshoot of phosphorylation and the subsequent activation of DNA topoisomerase II, the production of HIV-1 started. Applying three new protein kinase C inhibitors from the class of O-alkylglycerophospholipids we demonstrated that inhibition of protein kinase C-mediated phosphorylation of DNA topoisomerase II resulted in an inhibition of HIV-1 production. Based on the differential effect of the two protein kinase C activators, phorbol ester and bryostatin, we conclude that phosphorylation …

T-LymphocytesMitogen-activated protein kinase kinaseIn Vitro TechniquesMAP2K7Cell LineLactonesVirologyAnimalsPhosphorylationProtein kinase AProtein kinase CProtein Kinase CPharmacologybiologyCyclin-dependent kinase 2LysophosphatidylcholinesRats Inbred StrainsDNA topoisomerase II activityBryostatinsProtein kinase RMolecular biologyRatsDNA Topoisomerases Type Ibiology.proteinHIV-1Tetradecanoylphorbol AcetateCyclin-dependent kinase 9Electrophoresis Polyacrylamide GelMacrolidesAntiviral research
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Characterization of a T cell-derived lymphokine that acts synergistically with IL 3 on the growth of murine mast cells and is identical with IL4

1987

Abstract A mast cell-like cell line (SN-1) was established with the aid of growth factor(s) present in the supernatant of a Con A-stimulated L3T4 + T cell line. In analogy to other mast cell lines, IL 3 was identified as a growth factor for SN-1 cells. In addition, a second lymphokine produced by the T cells synergistically enhanced the IL 3-induced growth. This factor, originally termed mast cell growth enhancing factor (MaGEF), could be separated from IL 2, IL 3, a CSF-like activity and was purified to homogeneity. The N-terminal amino acid sequence (8 residues) and the functional properties of this lymphokine proved to be identical with those reported for BSF-1 (IL 4). Unless applied at …

T-Lymphocytesmedicine.medical_treatmentT cellImmunologyBiologyCell LineMicemedicineAnimalsImmunology and AllergyMast CellsInterleukin 4Interleukin 3InterleukinsGrowth factorLymphokineAntibodies MonoclonalHematologyMast cellMolecular biologyRecombinant ProteinsMolecular WeightCytokinemedicine.anatomical_structureCell cultureImmunologyElectrophoresis Polyacrylamide GelInterleukin-3Interleukin-4Immunobiology
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Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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Capillary electrophoretic and nuclear magnetic resonance studies of interactions between halophenols and ionic liquid or tetraalkylammonium cations.

2003

Aqueous capillary electrophoretic studies were performed to investigate interactions between halophenols and 1-ethyl-3-methylimidazolium tetrafluoroborate or tetraethylammonium tetrafluoroborate electrolytes. In both cases, increased halogen size correlated with increased affinity for the electrolyte cation. For isomers, the ortho substituted isomer exhibited higher affinity than the para isomer. Irreproducible CE results for analyte pairs in the presence of the ionic liquid stimulated investigations of the interactions between halophenols as well as with the cations of the electrolyte. These interactions were explored by proton and fluorine one-dimensional NMR. The NMR results indicated di…

TetraethylammoniumAqueous solutionChromatographyTetrafluoroborateMagnetic Resonance SpectroscopyChemistryOrganic ChemistryElectrophoresis CapillaryGeneral MedicineNuclear magnetic resonance spectroscopyElectrolyteBiochemistryAnalytical ChemistryHydrophobic effectQuaternary Ammonium Compoundschemistry.chemical_compoundCapillary electrophoresisHalogensPhenolsCationsIonic liquidJournal of chromatography. A
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Thermal Denaturation of Pea Globulins (Pisum sativum L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation

2013

The heat-induced denaturation and aggregation of mixed pea globulins (8%, w/w) were investigated using differential scanning calorimetry (DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC). DSC data showed that the pea proteins denaturation temperature (T(d)) was heating-rate dependent. The T(d) value decreased by about 4 °C by lowering the heating rate from 10 to 5 °C/min. The SDS-PAGE analysis revealed that protein denaturation upon heating at 90 °C was mainly governed by noncovalent interaction. The SEC-HPLC measurements indicated that low-denatured legumin (≈350-410 kDa) and vicilin/convicilin (≈170 kDa) globulins were heat-denatured and most of their subunits reassociated int…

Thermal denaturationProtein DenaturationHot TemperatureChromatographyCalorimetry Differential ScanningbiologyGlobulinProtein ConformationChemistryPeasfood and beveragesGlobulinsGeneral ChemistryProtein aggregationbiology.organism_classificationPisumSativumDifferential scanning calorimetrybiology.proteinLeguminElectrophoresis Polyacrylamide GelDenaturation (biochemistry)General Agricultural and Biological SciencesPlant ProteinsJournal of Agricultural and Food Chemistry
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