Search results for "serum albumin"

showing 10 items of 283 documents

Pancreatic insufficiency in celiac disease is not dependent on nutritional status

1994

To determine the relationship between pancreatic secretory capacity and nutritional status in celiac patients, we studied 52 patients with celiac disease (24 males, 28 females; age range 6-36 months) and 30 healthy control subjects (14 males, 16 females; age range 6-42 months). A secretin-cerulein test was performed on all patients, and levels of serum albumin and plasma fibronectin were assayed. In addition, weight/height ratios were calculated in the celiacs, who were then divided into three groups on this basis, as follows: celiacs with weight/height ratioor = 3rd percentile; those with weight/height ratio between the 4th and 10th percentiles; and those with weight/height ratio10th perce…

Malemedicine.medical_specialtyPercentilePhysiologyBiopsySerum albuminNutritional StatusDiseaseStatistics NonparametricPathogenesisSecretinInternal medicineIntestine SmallmedicineHumansProspective StudiesLipaseChi-Square DistributionbiologyChemistryGastroenterologyAlbuminInfantNutritional statusHepatologyCeliac DiseasePancreatic Function TestsEndocrinologyChild Preschoolbiology.proteinExocrine Pancreatic InsufficiencyFemaleCeruletideDigestive Diseases and Sciences
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Echinostoma caproni: kinetics of IgM, IgA and IgG subclasses in the serum and intestine of experimentally infected rats and mice.

2007

The kinetics of specific immunoglobulin M, A and IgG subclasses against Echinostoma caproni (Trematoda: Echinostomatidae) were analyzed in serum and intestinal fluid of two host species (Wistar rats and ICR mice) in which the course of the infection markedly differs. In rats, the worms were rapidly expelled, whereas E. caproni evokes in mice long-lasting infection. The pattern of antibody responses in both serum and intestinal samples was different in each host species. Serum responses in mice were characterized by significant increases of IgM, IgA, total IgG, IgG1 and IgG3, but not IgG2a. In contrast, serum responses in rats showed elevated levels of IgM, probably in relation to thymus-ind…

Malemedicine.medical_specialtyRatónImmunologyKineticsImmunoglobulinsEnzyme-Linked Immunosorbent AssayHost-Parasite InteractionsMiceRandom AllocationAntigenImmunityInternal medicineEchinostomaparasitic diseasesmedicineParasite hostingAnimalsRats WistarInterleukin 6Immunity MucosalSerum AlbuminEchinostomiasisMice Inbred ICRbiologyGeneral Medicinebiology.organism_classificationImmunoglobulin ARatsIntestinesInfectious DiseasesEndocrinologyImmunoglobulin MImmunoglobulin MImmunoglobulin GImmunologybiology.proteinParasitologyTrematodaExperimental parasitology
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Tuning protein adsorption on graphene surfaces via laser-induced oxidation

2021

An approach for controlled protein immobilization on laser-induced two-photon (2P) oxidation patterned graphene oxide (GO) surfaces is described. Selected proteins, horseradish peroxidase (HRP) and biotinylated bovine serum albumin (b-BSA) were successfully immobilized on oxidized graphene surfaces, via non-covalent interactions, by immersion of graphene-coated microchips in the protein solution. The effects of laser pulse energy, irradiation time, protein concentration and duration of incubation on the topography of immobilized proteins and consequent defects upon the lattice of graphene were systemically studied by atomic force microscopy (AFM) and Raman spectroscopy. AFM and fluorescence…

Materials scienceOxideBioengineering02 engineering and technology010402 general chemistry01 natural sciencesHorseradish peroxidaselaw.inventionsymbols.namesakechemistry.chemical_compoundlawFluorescence microscopeGeneral Materials ScienceBovine serum albuminbiologyGrapheneGeneral EngineeringGeneral Chemistry021001 nanoscience & nanotechnologyAtomic and Molecular Physics and Optics0104 chemical sciencesChemical engineeringchemistryBiotinylationbiology.proteinsymbols0210 nano-technologyRaman spectroscopyProtein adsorptionNanoscale Advances
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Multifunctional clickable and protein-repellent magnetic silica nanoparticles

2016

Silica nanoparticles are versatile materials whose physicochemical surface properties can be precisely adjusted. Because it is possible to combine several functionalities in a single carrier, silica-based materials are excellent candidates for biomedical applications. However, the functionality of the nanoparticles can get lost upon exposure to biological media due to uncontrolled biomolecule adsorption. Therefore, it is important to develop strategies that reduce non-specific protein-particle interactions without losing the introduced surface functionality. Herein, organosilane chemistry is employed to produce magnetic silica nanoparticles bearing differing amounts of amino and alkene func…

Materials scienceSurface PropertiesSilicon dioxideNanoparticleNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesMagneticschemistry.chemical_compoundAdsorptionDynamic light scatteringAnimalsGeneral Materials Sciencechemistry.chemical_classificationBiomoleculeSerum Albumin BovineSilicon Dioxide021001 nanoscience & nanotechnologyDynamic Light ScatteringFerrosoferric Oxide0104 chemical sciencesElectrophoresischemistryCovalent bondThermogravimetryNanoparticlesPolystyrenesCattleElectrophoresis Polyacrylamide GelMuramidaseAdsorption0210 nano-technologyProtein adsorptionNanoscale
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Porous Aluminium Oxide Coating for the Development of Spectroscopic Ellipsometry Based Biosensor: Evaluation of Human Serum Albumin Adsorption

2020

An electrochemically synthesised porous anodic aluminium oxide (pAAO) layer has been analysed by means of spectroscopic ellipsometry. The determined thickness of the formed pAAO layer obtained from spectroscopic ellipsometry measurements and modelling was 322.75 &plusmn

Materials scienceporous aluminium oxide02 engineering and technology010402 general chemistry01 natural sciencesspectroscopic ellipsometryoptical biosensorschemistry.chemical_compoundAdsorptionDesorptionMaterials ChemistrymedicineSurfaces and InterfacesBuffer solution021001 nanoscience & nanotechnologyHuman serum albumin0104 chemical sciencesSurfaces Coatings and FilmsNanoporechemistrylcsh:TA1-2040human serum albuminAluminium oxidespectroscopic ellipsometry ; human serum albumin ; porous aluminium oxide ; optical biosensorslcsh:Engineering (General). Civil engineering (General)0210 nano-technologyBiosensorLayer (electronics)Nuclear chemistrymedicine.drugCoatings
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Role of membrane dynamics processes and exogenous molecules in cellular resveratrol uptake: consequences in bioavailability and activities.

2011

In the fields of nutrition prevention and therapy treatment, numerous studies have reported interesting properties of trans-resveratrol (RSV), a natural polyphenol against pathologies such as vascular diseases, cancers, viral infections and neurodegenerative processes. These beneficial effects are supported by more studies showing the pleiotropic actions of RSV. Nevertheless, a crucial question concerning these effects is how the polyphenol, when applied to an organism, gains access to its targets. In this review, we focus on the biochemical and biological parameters involved in RSV transport, particularly the role of the phospholipid bilayer in RSV uptake (passive diffusion, carrier-mediat…

Membrane FluidityvirusesLipoproteinsIntegrinEstrogen receptorBiological AvailabilityResveratrolEndocytosischemistry.chemical_compoundMembrane LipidsMembrane MicrodomainsCell surface receptorStilbenesAnimalsHumansReceptorLipid raftbiologyCell MembraneFatty Acidsvirus diseasesBiological TransportSerum Albumin Bovinerespiratory systemIntegrin alphaVbeta3EndocytosisCell biologyBiochemistrychemistryResveratrolbiology.proteinIntracellularFood ScienceBiotechnologyMolecular nutritionfood research
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Micro- and mesoscopic process interactions in protein coagulation

2000

It has recently been recognized that pathological protein coagulation is responsible for lethal pathologies as diverse as amyloidosis, Alzheimer and TSE. Understanding the coagulation mechanisms is therefore stirring great interest. In previous studies we have shown that on profoundly different systems coagulation is the result of a strong interaction between two processes on different length scales (mesoscopic and microscopic). Here we report experiments on bovine serum albumin (BSA) showing that the overall mechanism is the result of at least 3 distinct and strongly intertwined processes, on both length scales: molecular conformational changes, solution demixing and intermolecular crossli…

Mesoscopic physicsPatient diagnosisbiologyBiochemistryMechanism (biology)ChemistryIntermolecular forcebiology.proteinBiophysicsCoagulation (water treatment)Statistical mechanicsBovine serum albuminProtein coagulationAIP Conference Proceedings
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Variation of the glycosylation pattern in MUC1 glycopeptide BSA vaccines and its influence on the immune response.

2012

Mice Inbred BALB CVaccinesGlycosylationGlycosylationMolecular StructureAntigen-antibody reactionsInjections SubcutaneousMucinMucin-1GlycopeptidesSerum Albumin BovineGeneral ChemistryCatalysisGlycopeptideAntigen-Antibody Reactionschemistry.chemical_compoundMiceImmune systemchemistryBiochemistryCell cultureCell Line TumorAnimalsHumansMUC1Angewandte Chemie (International ed. in English)
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Self-assembling of poly(aspartic acid) with bovine serum albumin in aqueous solutions

2016

Abstract Macromolecular co-assemblies built up in aqueous solutions, by using a linear polypeptide, poly(aspartic acid) (PAS), and a globular protein, bovine serum albumin (BSA), have been studied. The main interest was to identify the optimum conditions for an interpenetrated complex formation in order to design materials suitable for biomedical applications, such as drug delivery systems. BSA surface possesses several amino- and carboxylic groups available for covalent modification, and/or bioactive substances attachment. In the present study, mixtures between PAS and BSA were investigated at 37 °C in dilute aqueous solution by viscometry, dynamic light scattering and zeta potential deter…

Models MolecularProtein ConformationGlobular protein02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryDynamic light scatteringStructural BiologyAspartic acidZeta potentialAnimalsBovine serum albuminMolecular Biologychemistry.chemical_classificationAqueous solutionChromatographybiologyChemistryWaterSerum Albumin BovineGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnology0104 chemical sciencesSolutionsDrug deliverybiology.proteinCattlePeptides0210 nano-technologyProtein BindingNuclear chemistryMacromoleculeInternational Journal of Biological Macromolecules
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Evidence for Water-Tuned Structural Differences in Proteins: An Approach Emphasizing Variations in Local Hydrophilicity

2012

We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have re…

Models MolecularProtein StructureMedical PhysicsNon-Clinical MedicineProtein ConformationMaterials ScienceBiophysicsMolecular Conformationlcsh:MedicineElectronsLigandsBiochemistryPhysical ChemistryAnalytical ChemistryMacromolecular Structure AnalysisAnimalsHumanslcsh:ScienceBiologySerum AlbuminQuantum MechanicsPhysicslcsh:RFatty AcidsElectron Spin Resonance SpectroscopyProteinsComputational BiologyWaterSerum Albumin BovineProtein Structure Tertiarybody regionsChemistrySpectrophotometryInterdisciplinary PhysicsMedicinelcsh:QMaterials CharacterizationCattleMedicinal ChemistryHydrophobic and Hydrophilic InteractionsResearch ArticleProtein BindingPLoS ONE
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