Search results for "erythrocyte"

showing 10 items of 370 documents

Involvement of carboxyl groups in chloride transport and reversible DIDS binding to band 3 protein in human erythrocytes

2011

AbstractNoncovalent DIDS binding to Band 3 (AE1) protein in human erythrocyte membranes, modified by non-penetrating, water soluble 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)-carbodiimide iodide (EAC), was studied at 0°C in the presence of 165 mM KCl. Under experimental conditions applied up to (48 ± 5) % of irreversible chloride self-exchange inhibition was observed. The apparent dissociation constant, KD, for “DIDS-Band 3” complex, determined from the chloride transport experiments, was (34 ± 3) nM and (80 ± 12) nM for control and EAC-treated resealed ghosts, respectively. The inhibition constant, Ki, for DIDS was (35 ± 6) nM and (60 ± 8) nM in control and EAC-treated ghosts, respectively. T…

ErythrocytesIodideDissociation constant44'-Diisothiocyanostilbene-22'-Disulfonic AcidTritiumBiochemistryChloridechemistry.chemical_compoundCarbodiimideChloridesAnion Exchange Protein 1 ErythrocytemedicineHumansBinding siteErythrocyte membraneMolecular BiologyBand 3Ion transporterchemistry.chemical_classificationStilbenedisulfonateBinding SitesIon TransportbiologyCooperative bindingCell BiologyDissociation constantBand 3CrystallographyCarbodiimidesKineticsBiochemistrychemistryDIDSbiology.proteinmedicine.drugResearch ArticleProtein BindingCellular & Molecular Biology Letters
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Importance of Factors H and I for the Adherence of C3b-Coated Erythrocytes to Cells

1983

Abstract The role of cell membrane-associated human factor H for the binding of cell-bound Cab to complement receptor-carrying (CR + ) cells was investigated. Pretreatment of CR + cells with antibodies to factor H inhibited the adherence of Cab-coated red cells to human tonsil lymphocytes (TL) and peripheral blood monocytes (Mo). The Cab receptor reactivity of human polymorphonuclear leucocytes (PMN) was not influenced and the one of Raji lymphoblastoid cells only slightly influenced; iC3b and Cad receptor reactivity was in no case affected. When diisopropylfluorophosphate (DFP) in a concentration of 0.1 mM was present during pretreatment of the CR + cells with anti H, the antibodies gained…

ErythrocytesIsoflurophateRosette Formationmedicine.drug_classLymphocyteComplement Pathway AlternativeImmunologyMonoclonal antibodyMonocytesImmunoglobulin Fab FragmentsComplement C3b Inactivator ProteinsmedicineAnimalsHumansImmunology and AllergyLymphocytesComplement ActivationbiologyChemistryLymphoblastfungifood and beveragesHematologyMolecular biologyReceptors ComplementComplement systemRaji cellmedicine.anatomical_structureBiochemistryComplement Factor HFactor HReceptors Complement 3bbiology.proteiniC3bRabbitsAntibodyImmunobiology
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Inhibitory activity of sphingomyelin on hemolytic activity of coelomic fluid of Holothuria polii (echinodermata)

1987

Abstract The hemolytic activity of coelomic fluid from Holothuria polii is specifically inhibited by sphingomyelin. This phospholipid is the constituent of the membrane which probably interacts with the hemolysin thereby leading to the lysis.

ErythrocytesLysisSea CucumbersImmunologyPhospholipidSettore BIO/05 - ZoologiaInhibitory postsynaptic potentialHemolysisMicrobiologychemistry.chemical_compoundmedicineAnimalsPhospholipidsComplement Inactivator ProteinsBacteriabiologyHemolysinbiology.organism_classificationBody FluidsSphingomyelinsRed blood cellCholesterolSphingomyelin Phosphodiesterasemedicine.anatomical_structurechemistryBiochemistryCoelomlipids (amino acids peptides and proteins)SphingomyelinHolothuriaEchinodermataDevelopmental Biology
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New pegylated polyaspartamide-based polyplexes as gene delivery vectors

2010

Aims: To synthesize novel polyhydroxyethylaspartamide (PHEA) copolymers containing spermine (Spm) and polyethylene glycol (PEG) moieties in high yields, with the expectation that this material would show stealth properties and the ability to complex DNA by electrostatic interactions. Materials & methods: PHEA–PEG–Spm copolymer was prepared with a two-step reaction. Chemical, physicochemical and biological characterizations of PHEA–PEG–Spm copolymers and their obtained polyplexes with pDNA were performed. Results: The introduction of spermine in PHEA structure allows to obtain a copolymer bearing in the side chains polyamine moieties capable to interact with DNA. On the other hand, the …

ErythrocytesMaterials scienceBiocompatibilityGenetic VectorsStatic ElectricityGENE DELIVERY VECTORS POLYPLEXES NANOMEDICINE.Melanoma ExperimentalBiomedical EngineeringMedicine (miscellaneous)SpermineBioengineeringPolyethylene glycolDevelopmentGene deliveryPolyethylene GlycolsElectrolytesMicechemistry.chemical_compoundPolymer chemistryPEG ratioPolyaminesSide chainCopolymerAnimalsHumansNanotechnologyGeneral Materials SciencefungiGene Transfer Techniquestechnology industry and agricultureDNACombinatorial chemistryModels ChemicalchemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoSperminePeptidesPolyamineNanomedicine
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Phase-shifting by means of an electronically tunable lens: quantitative phase imaging of biological specimens with digital holographic microscopy

2016

The use of an electronically tunable lens (ETL) to produce controlled phase shifts in interferometric arrangements is shown. The performance of the ETL as a phase-shifting device is experimentally validated in phase-shifting digital holographic microscopy. Quantitative phase maps of a section of the thorax of a Drosophila melanogaster fly and of human red blood cells have been obtained using our proposal. The experimental results validate the possibility of using the ETL as a reliable phase-shifter device.

ErythrocytesMaterials scienceHolographyPhase (waves)01 natural scienceslaw.invention010309 opticsBiological specimenOpticsPhase shifting interferometrylawImage Interpretation Computer-Assisted0103 physical sciencesAnimalsHumans010302 applied physicsbusiness.industryAtomic and Molecular Physics and OpticsÒptica Aparells i instrumentsLens (optics)InterferometryMicroscòpiaDrosophila melanogasterPhase imagingDigital holographic microscopyBiological imagingbusiness
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Accurate single-shot quantitative phase imaging of biological specimens with telecentric digital holographic microscopy

2014

The advantages of using a telecentric imaging system in digital holographic microscopy (DHM) to study biological specimens are highlighted. To this end, the performances of nontelecentric DHM and telecentric DHM are evaluated from the quantitative phase imaging (QPI) point of view. The evaluated stability of the microscope allows single-shot QPI in DHM by using telecentric imaging systems. Quantitative phase maps of a section of the head of the drosophila melanogaster fly and of red blood cells are obtained via single-shot DHM with no numerical postprocessing. With these maps we show that the use of telecentric DHM provides larger field of view for a given magnification and permits more acc…

ErythrocytesMaterials scienceMicroscopeHolographyBiomedical EngineeringHolographyMagnificationImage processinglaw.inventionBiomaterialsBiological specimenOpticslawMicroscopyImage Processing Computer-AssistedAnimalsMicroscopybusiness.industryÒpticaAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsÒptica Aparells i instrumentsDrosophila melanogasterDigital holographic microscopybusinessHeadDigital holography
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Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin

2013

Pyolysin (PLO) belongs to the homologous family of the cholesterol- dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or proteolytic fragments that span domain 4 of the CDCs streptolysin O and perfringolysin O bind to membranes but fail to oligomerize, and they inhibit the activity of the respective wild-type toxins. We repo…

ErythrocytesMembrane bindingCellprotein bindingBiochemistryoligomerHemolysin Proteinschemistry.chemical_compoundReaction kineticsToxic materialsMonomersprotein domainRecombinant ProteinsHemolysisunclassified drugcytolysinmedicine.anatomical_structureMembraneBiochemistryStreptolysinsStreptolysinLarge sizeBacterial ToxinsBiologyCholesterol-dependent cytolysinHemolysisoligomerizationMembrane LipidsBacterial ProteinsProteolytic fragmentsEscherichia colimedicineAnimalsMonomer structuresMolecular BiologySheep Domesticcarboxy terminal sequenceC-terminal domainsCholesterolC-terminusCell MembraneHemolytic activitycholesterolCell Biologymedicine.diseaseProtein Structure TertiaryCell membranesKineticschemistryOligomersProtein MultimerizationPyolysinprotein pyolysinMembrane insertionCytology
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Graphene coating obtained in a cold-wall CVD process on the Co-Cr Alloy (L-605) for medical applications

2021

Graphene coating on the cobalt-chromium alloy was optimized and successfully carried out by a cold-wall chemical vapor deposition (CW-CVD) method. A uniform layer of graphene for a large area of the Co-Cr alloy (discs of 10 mm diameter) was confirmed by Raman mapping coated area and analyzing specific G and 2D bands

ErythrocytesMicroscopeScanning electron microscope02 engineering and technologyChemical vapor deposition01 natural scienceslaw.inventionlcsh:ChemistryMiceCoated Materials BiocompatibleCoatinglawMaterials TestingComposite materiallcsh:QH301-705.5SpectroscopySettore CHIM/02 - Chimica Fisicagraphene coating ; biocompatibility ; cobalt chromium alloy ; cold wall chemical vapor deposition methodGeneral Medicine021001 nanoscience & nanotechnologyMicrostructureBlood Coagulation FactorsComputer Science ApplicationsGraphitePartial Thromboplastin TimeBiocompatibility0210 nano-technologyLayer (electronics)Blood PlateletsMaterials scienceCell SurvivalSurface PropertiesPrimary Cell Cultureengineering.material010402 general chemistryCobalt-chromium alloyGraphene coatingCold-wall chemical vapor deposition methodArticleCatalysisInorganic ChemistryAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyGrapheneOrganic Chemistrytechnology industry and agricultureNanoindentationPlatelet Activation0104 chemical scienceslcsh:Biology (General)lcsh:QD1-999NIH 3T3 CellsengineeringChromium AlloysVolatilization
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Expression of Active Streptolysin O in Escherichia coli as a Maltose-Binding-Protein-Streptolysin-O Fusion Protein. The N-Terminal 70 Amino Acids are…

1996

Streptolysin 0 (SLO) is the prototype of a family of cytolysins that consists of proteins which bind to cholesterol and form very large transmembrane pores. Structure/function studies on the pore-forming cytolysin SLO have been complicated by the proteolytic inactivation of a substantial portion of recombinant SLO (rSLO) expressed in Escherichia coli. To overcome this problem, translational fusions between the E. coli maltose-binding protein (MBP) gene and SLO were constructed, using the vectors pMAL-p2 and pMAL-c2. MBP-SLO fusion proteins were degraded if secreted into the E. coli periplasm, but intact, soluble MBP-SLO fusion proteins were produced at high levels in the cytoplasm. Active S…

ErythrocytesMonosaccharide Transport Proteinsgenetic structuresProtein ConformationStreptococcus pyogenesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeHemolysisBiochemistryMaltose-Binding ProteinsStructure-Activity RelationshipMaltose-binding proteinProtein structureBacterial ProteinsEscherichia colimedicineHumansCloning MolecularEscherichia coliSequence DeletionPore-forming toxinBase SequencebiologyEscherichia coli ProteinsFluoresceinsFusion proteineye diseasesTransmembrane proteinBiochemistryLiposomesStreptolysinsbiology.proteinATP-Binding Cassette TransportersStreptolysinsense organsCytolysinCarrier ProteinsSequence AnalysisEuropean Journal of Biochemistry
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Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells.

1997

Staphylococcal α-toxin is a 293-residue, single-chain polypeptide that spontaneously assembles into a heptameric pore in target cell membranes. To identify the pore-forming domain, substitution mutants have been produced in which single cysteine residues were introduced throughout the toxin molecule. By attaching the environmentally sensitive dye acrylodan to the sulfhydryl groups, the environment of individual amino acid side chains could be probed. In liposomes, a single 23-amino acid sequence (residues 118–140) was found to move from a polar to a nonpolar environment, indicating that this sequence forms the walls of the pore. However, periodicity in side chain environmental polarity coul…

ErythrocytesNeutrophilsStaphylococcusT-LymphocytesBacterial ToxinsLipid BilayersBiologyHemolysin ProteinsCell membraneHemolysin ProteinsAdenosine TriphosphatePhagocytosismedicineAnimalsHumansCysteineLipid bilayerchemistry.chemical_classificationLiposomeMultidisciplinaryCell MembraneBiological SciencesFlow CytometryTransmembrane proteinRecombinant ProteinsAmino acidmedicine.anatomical_structureBeta barrelchemistryBiochemistryAmino Acid SubstitutionMutagenesis Site-DirectedPotassiumRabbitsCysteine
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