Search results for " Serum Albumin"

showing 10 items of 175 documents

Evidence for the presence of autoantibodies to the collagen-like portion of C1q in systemic lupus erythematosus.

1988

We investigated the connection between the C1q solid-phase binding assay (C1q SPBA) and double-stranded DNA antibodies, and analyzed the immune complex material in systemic lupus erythematosus (SLE) sera. Comparison with a new monoclonal assay for C1q-bearing immune complexes (the 242G3 assay) revealed that the immune complexes in SLE bind specifically to solid-phase C1q, and not to fluid-phase C1q. The C1q solid-phase binding activity sedimented as 7S IgG, was insensitive to DNase treatment, and could be selectively absorbed by C1q-coupled beads and by bovine serum albumin-anti-bovine serum albumin C1q beads, but not by DNA. Thus, antibodies to double-stranded DNA do not interfere in the C…

Complement Activating EnzymesImmunologySerum albuminchemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayAntigen-Antibody Complexurologic and male genital diseasesfluids and secretionsImmune systemRheumatologyimmune system diseasesComplement C1medicineImmunology and AllergyHumansLupus Erythematosus SystemicPharmacology (medical)Bovine serum albuminskin and connective tissue diseasesAutoantibodiesLupus erythematosusbiologybusiness.industryLigand binding assayComplement C1qAutoantibodyDNA Neoplasmmedicine.diseaseImmune complexImmunoglobulin GImmunologybiology.proteinCollagenAntibodybusinessUltracentrifugationArthritis and rheumatism
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Interacting processes in protein coagulation

1999

A strong interest is currently focused on protein self-association and deposit. This usually involves conformational changes of the entire protein or of a fragment. It can occur even at low concentrations and is responsible for pathologies such as systemic amyloidosis, Alzheimer's and Prion diseases, and other neurodegenerative pathologies. Readily available proteins, exhibiting at low concentration self-association properties related to conformational changes, offer very convenient model systems capable of providing insight into this class of problems. Here we report experiments on bovine serum albumin, showing that the process of conformational change of this protein towards an intermedia…

Conformational changeIntermediate formbiologyChemistryBiochemistrySystemic amyloidosisProtein coagulationBiochemistryStructural Biologybiology.proteinCoagulation (water treatment)Bovine serum albuminMolecular BiologyVolume concentrationProteins: Structure, Function, and Genetics
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Chiral separation of bupivacaine enantiomers by capillary electrophoresis partial-filling technique with human serum albumin as chiral selector

2004

Abstract Capillary electrophoresis (CE) is a powerful technique for enantiomer separations due to its intrinsic high separation efficiencies, speed of analysis, low reagent consumption and small sample requirements. However, some chiral selectors present strong background UV absorption providing high detection limits. The present paper deals with the application of the partial-filling technique to the separation of bupivacaine enantiomers by capillary electrophoresis using human serum albumin (HSA) as chiral selector. In this procedure the cationic surfactant cetyltrimethylammonium bromide (CTAB) was used as a dinamic capillary coating in order to reduce the electro-osmotic flow and detect …

Detection limitChromatographyChemistryCapillary actionOrganic ChemistryAnalytical chemistryElectrophoresis CapillaryStereoisomerismGeneral MedicineElectrolyteHuman serum albuminBupivacaineBiochemistryAnalytical ChemistryCapillary electrophoresisPharmaceutical PreparationsReagentmedicineAnesthetics LocalEnantiomerEnantiomeric excessmedicine.drugJournal of Chromatography A
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High-throughput capillary electrophoresis frontal analysis method for the study of drug interactions with human serum albumin at near-physiological c…

2004

The application of the short-end capillary injection to capillary electrophoresis frontal analysis (CE-FA) to study the interaction between basic, neutral and acid drugs towards human serum albumin (HSA) at near-physiological conditions is presented. The compounds selected display a wide range of binding affinities and the results obtained were in good agreement with those reported in the literature. An equation for the estimation of the number of primary binding sites and their corresponding affinity constants is developed isolating the experimentally measured variables in just one axis. The proposed CE-FA method to screen drug interactions with HSA under physiological conditions is simple…

DrugChromatographyChemistryDrug discoveryCapillary actionmedia_common.quotation_subjectClinical BiochemistryElectrophoresis CapillaryHuman serum albuminBiochemistryAnalytical ChemistryCapillary electrophoresisPharmaceutical PreparationsmedicineHumansBinding siteAnalysis methodSerum AlbuminBinding affinitiesmedia_commonmedicine.drugElectrophoresis
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Characterization of basic drug–human serum protein interactions by capillary electrophoresis

2006

Drug-protein interactions are determining factors in the therapeutic, pharmacodynamic and toxicological drug properties. The affinity of drugs towards plasmatic proteins is apparently well established in bibliography. Albumin (HSA) especially binds neutral and negatively charged compounds; alpha(1)-acid glycoprotein (AGP) binds many cationic drugs, lipoproteins bind to nonionic and lipophilic drugs and some anionic drugs while globulins interact inappreciably with the majority of drugs. In this paper, the characterization of the interaction between cationic drugs, beta-blockers and phenotiazines towards HSA, AGP, and both HSA + AGP mixtures of proteins under physiological conditions by CE-f…

DrugGlobulinmedia_common.quotation_subjectAdrenergic beta-AntagonistsClinical BiochemistryThiazinesUltrafiltrationPlasma protein bindingBiochemistryAnalytical ChemistryCapillary electrophoresisPhenothiazinesmedicineHumansLabetalolSerum Albuminmedia_commonchemistry.chemical_classificationbiologyAlbuminElectrophoresis CapillaryBlood ProteinsOrosomucoidHuman serum albuminchemistryBiochemistryPindololbiology.proteinGlycoproteinDrug metabolismProtein Bindingmedicine.drugELECTROPHORESIS
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Distribution of chlorpromazine in a simplified blood influenced by various drugs

1973

The binding of chlorpromazine to erythrocytes and to albumin as influenced by other drugs was studied in a simplified blood (31.5±0.3% bovine erythrocytes, 4 g-% bovine serum albumin in 0.02 M phosphate buffer solution containing 0.15 M NaCl). the total concentration of chlorpromazine in the simplified blood was 10−4 M, the concentration of the displacing drugs was 10−3 M. After an incubation period of 3 h at 22° C the chlorpromazine concentration was determined in the albumin solution after centrifugation of the blood at 3000×g and in the aqueous phase after ultracentrifugation at 150000×g. Under control conditions 68.1±0.9% of chlorpromazine was bound to the erythrocytes, 28.5±0.9% was bo…

ErythrocytesChlorpromazineIndomethacinSuraminBenzoatesBinding CompetitiveIncubation periodCoumarinsmedicineAnimalsDistribution (pharmacology)CentrifugationThiopentalBovine serum albuminChlorpromazinePharmacologySulfonamidesBinding SitesChromatographyQuininebiologyProbenecidChemistryFatty AcidsAqueous two-phase systemAlbuminSerum Albumin BovineGeneral MedicineChlorothiazideTetracyclineAntidepressive AgentsSalicylatesAcetazolamidePhenylbutazoneSolubilityPhenytoinbiology.proteinCattleUltracentrifugeDeoxycholic AcidProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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In vivo survival rate of rabbit morulae after vitrification in a medium without serum protein.

2000

The in vivo survival rate of rabbit morulae after vitrification in a mixture of dimethyl sulphoxide and ethylene glycol solution without protein supplement (WPS) was compared with two types of protein supplements: rabbit serum (RS) and bovine serum albumin (BSA). Significant dif- ferences were observed in the percentage of transferable embryos (undamaged embryos after devit- rification, 80.4 % versus 93.2 and 92.1 %, WPS, BSA and RS, respectively, P < 0.05) and live born rate (40.9 % versus 56.1 %, WPS and BSA, respectively, P < 0.05). Non-significant differences were, however, observed in the percentages of implanted embryos at 12 days post-ovulation induc- tion (56.7, 69.7 and 68.6 %), po…

Ethylene GlycolMorulaAndrologychemistry.chemical_compoundCryoprotective AgentsPregnancyIn vivo[SDV.BDD] Life Sciences [q-bio]/Development BiologyAnimalsDimethyl SulfoxideVitrificationEmbryo ImplantationBovine serum albuminFetal DeathSurvival rate[SDV.BDLR] Life Sciences [q-bio]/Reproductive BiologyCryopreservationLagomorphabiologySerum Albumin BovineEmbryo cultureBlood ProteinsEmbryo Transferbiology.organism_classificationEmbryo transfer[SDV.AEN] Life Sciences [q-bio]/Food and NutritionBloodchemistryBiochemistrybiology.proteinFemaleRabbitsEthylene glycol
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Ligand-Binding Cooperativity Effects in Polymer-Protein Conjugation.

2019

We present an electron paramagnetic resonance (EPR) spectroscopic characterization of structural and dynamic effects that stem from post-translational modifications of bovine serum albumin (BSA), an established model system for polymer-protein conjugation. Beyond the typical drug delivery and biocompatibility aspect of such systems, we illustrate the causes that alter internal dynamics and therefore functionality in terms of ligand-binding to the BSA protein core. Uptake of the paramagnetic fatty acid derivative 16-doxyl stearic acid by several BSA-based squaric acid macroinitiators and polymer-protein conjugates was studied by EPR spectroscopy, aided by dynamic light scattering (DLS) and z…

Ethylene GlycolPolymers and PlasticsPolymersBioengineeringCooperativity02 engineering and technology010402 general chemistryLigands01 natural scienceslaw.inventionPolyethylene GlycolsBiomaterialsCyclic N-Oxideschemistry.chemical_compoundDrug Delivery SystemsDynamic light scatteringlawMaterials ChemistryZeta potentialBovine serum albuminElectron paramagnetic resonanceBinding SitesbiologyElectron Spin Resonance SpectroscopySerum Albumin Bovine021001 nanoscience & nanotechnologyLigand (biochemistry)Dynamic Light Scattering0104 chemical scienceschemistrybiology.proteinBiophysicsSurface modificationMethacrylates0210 nano-technologyEthylene glycolBiomacromolecules
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2014

This study was performed to explore the feasibility of tracing nanoparticles for drug transport in the healthy rat brain with a clinical MRI scanner. Phantom studies were performed to assess the R1 ( =  1/T1) relaxivity of different magnetically labeled nanoparticle (MLNP) formulations that were based on biodegradable human serum albumin and that were labeled with magnetite of different size. In vivo MRI measurements in 26 rats were done at 3T to study the effect and dynamics of MLNP uptake in the rat brain and body. In the brain, MLNPs induced T1 changes were quantitatively assessed by T1 relaxation time mapping in vivo and compared to post-mortem results from fluorescence imaging. Followi…

Fluorescence-lifetime imaging microscopyMultidisciplinarymedicine.diagnostic_testbiologyChemistryCentral nervous systemSerum albuminNanoparticleMagnetic resonance imaging02 engineering and technology021001 nanoscience & nanotechnologyHuman serum albumin030218 nuclear medicine & medical imaging03 medical and health sciences0302 clinical medicinemedicine.anatomical_structureIn vivomedicinebiology.protein0210 nano-technologyDrug carrierBiomedical engineeringmedicine.drugPLOS ONE
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RAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagy

2014

Macroautophagy is a degradative pathway that sequesters and transports cytosolic cargo in autophagosomes to lysosomes, and its deterioration affects intracellular proteostasis. Membrane dynamics accompanying autophagy are mostly elusive and depend on trafficking processes. RAB GTPase activating proteins (RABGAPs) are important factors for the coordination of cellular vesicle transport systems, and several TBC (TRE2-BUB2-CDC16) domain-containing RABGAPs are associated with autophagy. Employing C. elegans and human primary fibroblasts, we show that RAB3GAP1 and RAB3GAP2, which are components of the TBC domain-free RAB3GAP complex, influence protein aggregation and affect autophagy at basal an…

GTPase-activating proteinlipid dropletsrab3 GTP-Binding ProteinsATG16L1DMSO dimethyl sulfoxideFEZ20302 clinical medicineATG autophagy-relatedPhagosomesDAPI 4’ 6-diamidino-2-phenylindoleSQSTM1 sequestosome 1ATG16L1MAP1LC3 microtubule-associated protein 1 light chain 3GFP green fluorescent protein0303 health sciencesGABARAP GABA(A) receptor-associated proteinGTPase-Activating ProteinsCell biologyRAB3GAP1RAB3GAP2RABGAP RAB GTPase activating proteinATG3autophagyCALCOCO2 calcium binding and coiled-coil domain 2Basic Research PaperseV empty vectorATG8ATG5PBS phosphate-buffered salineBiologyPE phosphatidylethanolamineTBC domain TRE2-BUB2-CDC16 domainBAG3GEF guanine nucleotide exchange factor03 medical and health sciencesC. elegans Caenorhabditis elegansAnimalsHumansCaenorhabditis elegansMolecular Biology030304 developmental biologySirolimusDPH 1 6-diphenyl-1 3 5-hexatrieneproteostasisAutophagyBiological TransportCell BiologyFEZ1Bafi bafilomycin A1FEZ fasciculation and elongation protein zetaNBR1 neighbor of BRCA1 gene 1ProteostasissiRNA small interfering RNABSA bovine serum albuminRabLysosomes030217 neurology & neurosurgeryAutophagy
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