Search results for "light"

showing 10 items of 3575 documents

Processing of tetanus and botulinum A neurotoxins in isolated chromaffin cells.

1995

Tetanus and botulinum A neurotoxins were introduced into the cytosol of chromaffin cells by means of an electric field in which the plasma membrane is forced to form pores of approximately 1 micron at the sites facing the electrodes. As demonstrated by electron microscopy, both [125I] and gold-labelled tetanus toxin (TeTx) diffuse through these transient openings. Dichain-TeTx, with its light chain linked to the heavy chain by means of a disulfide bond, causes the block of exocytosis to develop more slowly than does the purified light chain. The disulfide bonds, which in both toxins hold the subunits together, were cleaved by the intrinsic thioredoxin-reductase system. Single chain TeTx, in…

ProteasesBotulinum ToxinsCell Membrane PermeabilityProteolysisImmunoglobulin light chainmedicine.disease_causeExocytosisExocytosisTetanus ToxinmedicinePeptide bondAnimalsCells CulturedPharmacologymedicine.diagnostic_testToxinChemistryGeneral MedicineCytosolMicroscopy ElectronElectroporationBiochemistryAdrenal MedullaBiophysicsMicroscopy Electron ScanningCattleIntracellularNaunyn-Schmiedeberg's archives of pharmacology
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Aggregation Kinetics of Bovine Serum Albumin Studied by FTIR Spectroscopy and Light Scattering

2003

To investigate which type of structural and conformational changes is involved in the aggregation processes of bovine serum albumin (BSA), we have performed thermal aggregation kinetics in D(2)O solutions of this protein. The tertiary conformational changes are followed by Amide II band, the secondary structural changes and the formation of beta-aggregates by the Amide I' band and, finally, the hydrodynamic radius of aggregates by dynamic light scattering. The results show, as a function of pD, that: tertiary conformational changes are more rapid as pD increases; the aggregation proceeds through formation of ordered aggregates (oligomers) at pD far from the isoelectric point of the protein;…

Protein ConformationKineticsBiophysicsProtein aggregationBiochemistryProtein Structure SecondaryProtein structureDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationStatic light scatteringDeuterium OxideBovine serum albuminInfrared spectroscopyStatic light scatteringbiologyChemistryOrganic ChemistryTemperatureSerum Albumin BovineConformational changeRandom coilProtein tertiary structureKineticsCrystallographyBovine serum albuminbiology.proteinDynamic light scatteringCattleProtein aggregation
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Molecular mass of macromolecules and subunits and the quaternary structure of hemoglobin from the microcrustacean Daphnia magna

2006

The molecular masses of macromolecules and subunits of the extracellular hemoglobin from the fresh-water crustacean Daphnia magna were determined by analytical ultracentrifugation, multiangle laser light scattering and electrospray ionization mass spectrometry. The hemoglobins from hypoxia-incubated, hemoglobin-rich and normoxia-incubated, hemoglobin-poor Daphnia magna were analyzed separately. The sedimentation coefficient of the macromolecule was 17.4 +/- 0.1 S, and its molecular mass was 583 kDa (hemoglobin-rich animals) determined by AUC and 590.4 +/- 11.1 kDa (hemoglobin-rich animals) and 597.5 +/- 49 kDa (hemoglobin-poor animals), respectively, determined by multiangle laser light sca…

Protein DenaturationChromatography GasGlycosylationLightMacromolecular SubstancesProtein ConformationElectrospray ionizationProtein subunitDaphnia magnaMultiangle light scatteringBiologyBiochemistryHemoglobinsImaging Three-DimensionalAnimalsScattering RadiationProtein Structure QuaternaryMolecular BiologyChromatography High Pressure LiquidChromatographyMolecular massLasersfungiCell BiologyHemoglobin Subunitsbiology.organism_classificationMolecular WeightProtein SubunitsDaphniaFemaleProtein quaternary structureHemoglobinFEBS Journal
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Conformational changes involved in thermal aggregation processes of bovine serum albumin

2003

We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circul…

Protein DenaturationCircular dichroismHot TemperatureLightKineticsSerum albuminBiophysicsProtein aggregationCircular dichroismBiochemistryProtein Structure SecondaryProtein structureAnimalsHumansScattering RadiationCysteineBovine serum albuminPhysical and Theoretical ChemistryProtein secondary structurebiologyChemistryOrganic ChemistryTryptophanSerum Albumin BovineFluoresceinsConformational changeProtein Structure TertiaryKineticsCrystallographySpectrometry FluorescenceBovine serum albuminSteady-state fluorescencebiology.proteinCattlesense organsProtein aggregationCysteine
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Thermal aggregation of beta-lactoglobulin in presence of metal ions.

2007

In this work, we report a study of the effects of zinc and copper ions on the heat-induced aggregation of beta-lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FTIR absorption measurements show the different role played by the two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than copper. Then, at fixed temperature, formation of a large amount of aggregates, of large dimension, is observed for Zn-BLG in shorter time; on the contrary, the presence of copper in solution does not affect the aggregation proc…

Protein DenaturationHot TemperatureCations DivalentMetal ions in aqueous solutionKineticsInorganic chemistryBiophysicsBeta-lactoglobulinchemistry.chemical_elementZincLactoglobulinsProtein aggregationBiochemistryProtein Structure SecondaryDivalentSpectroscopy Fourier Transform InfraredAnimalsMetal ionProtein secondary structurechemistry.chemical_classificationOrganic ChemistryLight scatteringCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)FTIR spectroscopyKineticsZincchemistryChemical engineeringCattleAbsorption (chemistry)Protein aggregationCopperBiophysical chemistry
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Refolding of the integral membrane protein light-harvesting complex II monitored by pulse EPR

2009

The major light-harvesting chlorophyll a / b complex (LHCII) of the photosynthetic apparatus in plants self-organizes in vitro. The recombinant apoprotein, denatured in dodecyl sulfate, spontaneously folds when it is mixed with its pigments, chlorophylls, and carotenoids in detergent solution, and assembles into structurally authentic LHCII in the course of several minutes. Pulse EPR techniques, specifically double-electron-electron resonance (DEER), have been used to analyze protein folding during this process. Pairs of nitroxide labels were introduced site-specifically into recombinant LHCII and shown not to affect the stability and function of the pigment-protein complex. Interspin dist…

Protein DenaturationProtein FoldingTime FactorsMultidisciplinaryPulsed EPRSuperhelixChemistryElectron Spin Resonance SpectroscopyLight-Harvesting Protein ComplexesPeasMembrane ProteinsElectronsBiological SciencesModels BiologicalProtein Structure SecondaryTransmembrane domainB vitaminsCrystallographyProtein structureMutationHelixSpin LabelsProtein foldingApoproteinsIntegral membrane proteinProceedings of the National Academy of Sciences
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Larval zebrafish proteome regulation in response to an environmental challenge

2019

Adaptation to the environment during development influences the life-long survival of an animal. While brain-wide proteomic changes are expected to underlie such experience-driven physiological and behavioral flexibility, a comprehensive overview of the nature and extent of the proteomic regulation following an environmental challenge during development is currently lacking. In this study, the brain proteome of larval zebrafish is identified and it is determined how it is altered by an exposure to a natural and physical environmental challenge, namely prolonged exposure to strong water currents. A comprehensive larval zebrafish brain proteome is presented here. Furthermore, 57 proteins that…

Proteomics0303 health sciencesProteome030302 biochemistry & molecular biologyBrainComputational biologyBiologyProteomicsbiology.organism_classificationBiochemistryFight-or-flight response03 medical and health sciencesLarvaNeuroplasticityProteomeZebrafish larvaeSpatial learningAnimalsAdaptationMolecular BiologyZebrafishZebrafish030304 developmental biology
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Insights in ChAdOx1 nCoV-19 vaccine-induced immune thrombotic thrombocytopenia

2021

Abstract SARS-CoV-2 vaccine ChAdOx1 nCoV-19 (AstraZeneca) causes a thromboembolic complication termed vaccine-induced immune thrombotic thrombocytopenia (VITT). Using biophysical techniques, mouse models, and analysis of VITT patient samples, we identified determinants of this vaccine-induced adverse reaction. Super-resolution microscopy visualized vaccine components forming antigenic complexes with platelet factor 4 (PF4) on platelet surfaces to which anti-PF4 antibodies obtained from VITT patients bound. PF4/vaccine complex formation was charge-driven and increased by addition of DNA. Proteomics identified substantial amounts of virus production-derived T-REx HEK293 proteins in the ethyle…

ProteomicsAntigen-Antibody ComplexPlatelet Factor 4Extracellular TrapsBiochemistryEpitopesMiceSinus Thrombosis IntracranialMedicinePlateletCell Line TransformedMicroscopybiologyHematologymedicine.anatomical_structureSpike Glycoprotein CoronavirusAntibodyDrug ContaminationVirus CultivationGenetic VectorsImmunologyAdenoviridaeProinflammatory cytokineImaging Three-DimensionalImmune systemAntigenChAdOx1 nCoV-19AnimalsHumansPlatelet activationB cellAutoantibodiesInflammationPurpura Thrombocytopenic IdiopathicSARS-CoV-2business.industryCOVID-19Cell BiologyPlatelet ActivationPlatelets and ThrombopoiesisDynamic Light ScatteringHEK293 CellsImmunoglobulin GImmunologybiology.proteinCapsid ProteinsbusinessCapillary Leak SyndromePlatelet factor 4Extravasation of Diagnostic and Therapeutic MaterialsBlood
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Cellular effects of bacterial N-3-Oxo-dodecanoyl-L-Homoserine lactone on the sponge Suberites domuncula (Olivi, 1792): insights into an intimate inte…

2014

International audience; Sponges and bacteria have lived together in complex consortia for 700 million years. As filter feeders, sponges prey on bacteria. Nevertheless, some bacteria are associated with sponges in symbiotic relationships. To enable this association, sponges and bacteria are likely to have developed molecular communication systems. These may include molecules such as N-acyl-L-homoserine lactones, produced by Gram-negative bacteria also within sponges. In this study, we examined the role of N-3-oxododecanoyl-L-homoserine lactone (3-oxo-C12-HSL) on the expression of immune and apoptotic genes of the host sponge Suberites domuncula. This molecule seemed to inhibit the sponge inn…

ProteomicsApoptosisPathogenesisPathology and Laboratory MedicineBiochemistrycaspase 74-Butyrolactonecaspase 3lcsh:ScienceCytoskeletoncaspase like 7 gene0303 health sciencesToll-like receptorMarine Ecologytoll like receptorGenomicsproto oncogeneEndocytosisCell biologySuberites domunculaCellular Structures and Organellesalpha actininCell signalingtoll like receptor associated factor 6Gram negative bacteriumparacrine signalingMicrobiology03 medical and health sciencesGeneticsRNA Messengerhost pathogen interactionprotein expressiontwo dimensional electrophoresisBacteria030306 microbiologyEcology and Environmental Scienceslcsh:RBiology and Life SciencesComputational BiologyImmunity Innatecarrier proteinSpongebacterial membranelcsh:Qimmunological toleranceSuberitesProtein AbundanceSuberitessuberites domuncula[SDV]Life Sciences [q-bio]lcsh:MedicineMolecular Cell BiologyMedicine and Health Sciencesinnate immunityperforinMultidisciplinaryEcologybiologymessenger RNAarticlecell communicationAnimal Modelsmatrix assisted laser desorption ionization time of flight mass spectrometryunclassified drugPoriferaHost-Pathogen InteractionscytotoxicityactinTranscriptome Analysishormone actionResearch ArticleSymbiotic bacteriaprotein bcl 2Marine BiologycofilinResearch and Analysis Methodsn (3 oxododecanoyl)homoserine lactoneMicrobial EcologycogninModel OrganismsHomoserineAnimalscontrolled study14. Life underwatergeneSymbiosiscell viabilityadenosine triphosphatase030304 developmental biologynonhumanChemical EcologyMembrane ProteinsCell Biologytumor necrosis factor receptor associated factor 6Genome Analysisbiology.organism_classificationalpha tubulinGene Expression RegulationMembrane proteingene expressioncaspase like 3 geneGenome Expression AnalysisBacteriaPLoS ONE
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Photomagnetism of Molecular Systems

2001

This article reviews various classes of transition metal compounds which display in the solid state light sensitive electronic structure modifications accompanied by drastic changes of their magnetic and/or optical properties, i.e., photomagnetism. Selected examples from this rapidly expanding field, include spin crossover, stilbenoid and nitrosyl complexes, as well as Prussian blue analogues.

Prussian bluechemistry.chemical_compoundTransition metalchemistrySpin crossoverInorganic chemistryLight sensitiveElectronic structureMolecular systemsPhotochemistryPhotomagnetismLIESST
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