Search results for "serum albumin"

showing 10 items of 283 documents

Circulating specific antibodies enhance systemic cross-priming by delivery of complexed antigen to dendritic cells in vivo

2012

Increasing evidence suggests that antibodies can have stimulatory effects on T-cell immunity. However, the contribution of circulating antigen-specific antibodies on MHC class I cross-priming in vivo has not been conclusively established. Here, we defined the role of circulating antibodies in cross-presentation of antigen to CD8(+) T cells. Mice with hapten-specific circulating antibodies, but naϊve for the T-cell antigen, were infused with haptenated antigen and CD8(+) T-cell induction was measured. Mice with circulating hapten-specific antibodies showed significantly enhanced cross-presentation of the injected antigen compared with mice that lacked these antibodies. The enhanced cross-pre…

Cellular immunityOvalbuminImmunologyMice Transgenicchemical and pharmacologic phenomenaAntigen-Antibody ComplexCD8-Positive T-LymphocytesBiologyDendritic cellsAntibodiesMiceCross-PrimingImmune systemAntigenAntigens NeoplasmMHC class ITcellsAnimalsImmunology and AllergyImmunity CellularB cellsCross-presentationHistocompatibility Antigens Class ICross-presentationSerum Albumin BovineFlow CytometryCD11c AntigenMice Inbred C57BLMacrophage-1 antigenHumoral immunityImmunologybiology.proteinAntibodyHaptensEuropean Journal of Immunology
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Albumin binding and hydrophobic character of promazine and chlorpromazine metabolites.

1972

1. The binding of didesmethylpromazine, promazine N-oxide, 2-hydroxypromazine, promazine sulfoxide, monodesmethylpromazine sulfoxide, didesmethylchlorpromazine, chlorpromazine N-oxide, and chlorpromazine sulfoxide to bovine serum albumin was determined by means of sephadex gel filtration. 2. The albumin binding of these substances was characterized by the following parameters: the percentage α of free substance, the percentage β of bound substance, the binding constants K1, k+ and m, the number of binding sites per albumin molecule, and the free binding energy ΔFo. 3. The partition coefficients between n-octanol and buffer solution, pH 7.40, were measured for the above mentioned metabolites…

Chemical PhenomenaChlorpromazineStatistics as TopicPlasma protein bindingchemistry.chemical_compoundmedicineAnimalsBovine serum albuminChlorpromazinePromazinePromazinePharmacologyChromatographyBinding SitesbiologyAlbuminSulfoxideSerum Albumin BovineGeneral MedicineBuffer solutionChemistrychemistrySolubilitySephadexSulfoxidesbiology.proteinChromatography GelCattleNitrogen OxidesChlorinemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Cationized albumin-biocoatings for the immobilization of lipid vesicles

2010

Tethered lipid membranes or immobilized lipid vesicles are frequently used as biomimetic systems. In this article, the authors presented a suitable method for efficient immobilization of lipid vesicles onto a broad range of surfaces, enabling analysis by quantitative methods even under rigid, mechanical conditions-bare surfaces such as hydrophilic glass surfaces as well as hydrophobic polymer slides or metal surfaces such as gold. The immobilization of vesicles was based on the electrostatic interaction of zwitterionic or negatively charged lipid vesicles with two types of cationic chemically modified bovine serum albumin (cBSA) blood plasma proteins (cBSA-113 and cBSA-147). Quantitative an…

Chemistry(all)Surface PropertiesAnalytical chemistryGeneral Physics and AstronomyPhysics and Astronomy(all)Microscopy Atomic ForceGeneral Biochemistry Genetics and Molecular BiologyBiomaterialsCoated Materials BiocompatibleMaterials Science(all)CationsZeta potentialGeneral Materials ScienceBovine serum albuminSurface plasmon resonanceLiposomebiologyChemistryBiochemistry Genetics and Molecular Biology(all)VesicleSerum Albumin BovineGeneral ChemistryAdhesionMembraneLiposomesBiophysicsbiology.proteinAdsorptionProtein adsorptionProtein BindingBiointerphases
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Femtosecond Transient Absorption Study of the Dynamics of Acrylodan in Solution and Attached to Human Serum Albumin

2003

The excited-state relaxation dynamics of the protein-labeling dye acrylodan in solution and attached to human serum albumin has been studied by femtosecond transient absorption spectroscopy. Time-resolved spectra and kinetics of stimulated emission and excited-state absorption in the wavelength region from 400 to 800 nm were studied in ethanol and dimethylformamide. The excited-state solvation dynamics is characterized by multiexponential behavior in both solvents. In ethanol solution, the time dependence of the transient spectra is interpreted in terms of fast solvent relaxation followed by excited-state isomerization of the dye. Acrylodan attached to the protein shows a relaxation compone…

ChemistryKineticsSolvationAnalytical chemistryHuman serum albuminPhotochemistryFluorescenceSurfaces Coatings and FilmsFemtosecondUltrafast laser spectroscopyMaterials ChemistrymedicineRelaxation (physics)Physical and Theoretical ChemistryAbsorption (chemistry)medicine.drugThe Journal of Physical Chemistry B
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Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.

2007

The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…

ChlorpheniramineClinical BiochemistryPlasma protein bindingPharmacologyBiochemistryAnalytical ChemistryPharmacokineticsOrphenadrinemedicineOrphenadrineHumansSerum AlbuminDrug CarriersChromatographyBinding SitesChemistryBiological activityStereoisomerismBrompheniramineHuman serum albuminBrompheniraminebody regionsHydroxyzineembryonic structuresHistamine H1 AntagonistsEnantiomerDrug carriermedicine.drugProtein BindingElectrophoresis
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Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.

1972

The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.

ChlorpropamideChlorpropamideSuraminTolbutamideSerum albuminSuraminIn Vitro TechniquesBenzoatesPhenprocoumonCoumarinsBenzyl CompoundsmedicineAnimalsBovine serum albuminPharmacologyChromatographyBinding SitesbiologyChemistryAlbuminAnticoagulantsDextransSerum Albumin BovineGeneral MedicineCarbutamideGlycolatesCarbutamideSulfonylurea CompoundsSephadexbiology.proteinChromatography GelIodobenzoatesCattlemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Characterization of antihistamine–human serum protein interactions by capillary electrophoresis

2007

An important topic in the drug discovery and development process is the role of drug binding to plasma proteins. In this paper the characterization of the interaction between antihistamines (cationic drugs) towards human serum albumin (HSA) and alpha(1)-acid glycoprotein (AGP) under physiological conditions by capillary electrophoresis-frontal analysis is presented. Furthermore, the binding of these drugs to all plasma proteins is evaluated by using ultrafiltration and capillary electrophoresis. Antihistamines present a wide-ranging behaviour with respect to their affinities towards plasma proteins. Orphenadrine, phenindamine, tripelenamine and tripolidine principally bind to HSA; carbinoxa…

ChromatographyPhenindamineChemistryOrganic ChemistryElectrophoresis CapillaryBlood ProteinsGeneral MedicinePlasma protein bindingBrompheniramineHuman serum albuminBiochemistryBlood proteinsAnalytical Chemistrychemistry.chemical_compoundChlorcyclizineBiochemistryDimetindeneHistamine H1 AntagonistsmedicineHumansCarbinoxamineProtein Bindingmedicine.drugJournal of Chromatography A
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Fast enantiomeric separation of propranolol by affinity capillary electrophoresis using human serum albumin as chiral selector: application to qualit…

2004

Abstract In the last years, capillary electrophoresis (CE) has gained considerable interest in pharmaceutical laboratories for controlling the chiral purity of drugs. This paper describes a simple and fast method for resolution of propranolol enantiomers by affinity capillary electrophoresis (ACE) using human serum albumin (HSA) as chiral selector. The effect of several experimental variables such as HSA concentration, temperature, chiral selector plug length and addition of organic modifiers, on the separation is evaluated. Complete enantioresolution of R- and S-propranolol was achieved in less than 5 min when the capillary was completely filled with 100 μM HSA solution and the electrophor…

ChromatographyResolution (mass spectrometry)biologyCapillary actionChemistrySerum albuminPropranololHuman serum albuminBiochemistryAnalytical ChemistryElectrophoresisCapillary electrophoresismedicinebiology.proteinEnvironmental ChemistryEnantiomerSpectroscopymedicine.drugAnalytica Chimica Acta
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Enrichment of proteinaceous materials on a strong cation-exchange diol silica restricted access material: protein–protein displacement and interactio…

2004

A study of size exclusion and enrichment of proteins employing strong cation-exchange diol silica restricted access material (SCX-RAM) under saturation conditions is presented. Experiments were carried out with bacitracin, protamine, ribonuclease, lysozyme and bovine serum albumin as individual proteinaceous analytes as well as comprehensive binary mixtures and with human urine samples. Protein size dependent capacity features of the SCX-RAM column was observed. Bacitracin demonstrated the highest capacity followed by protamine while adsorption capacities of both ribonuclease and lysozyme were found smaller by a factor of 10. Applying binary protein samples occurring displacement effects we…

ChromatographybiologyChemistryOrganic ChemistryIon chromatographySize-exclusion chromatographyProteinsGeneral MedicineSilicon DioxideBiochemistryProtamineAnalytical ChemistryGel permeation chromatographyProteinuriachemistry.chemical_compoundAdsorptionbiology.proteinHumansCation Exchange ResinsLysozymeBovine serum albuminPeptidesProtein adsorptionJournal of Chromatography A
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Application of Liquid-Liquid Partition Chromatography (LLPC) in the Preparation of Steroid Binding Proteins

1989

Two human serum proteins, i.e. sex hormone binding globulin (h-SHBG) and corticosteroid binding globulin (h-CBG), rat corticosteroid binding globulin (r-CBG), and progesterone binding globulin (PBG) from new guinea pig were purified by the application of three different modes of chromatography. The proteins were purified by affinity chromatography and anion exchange chromatography. Fractions containing the steroid binding proteins were finally purified by liquid-liquid partition chromatography on LiParGel 750 (Merck, Darmstadt, FRG). This Chromatographic sequence clearly separated the steroid binding proteins from other proteins, mainly from serum albumin without a loss of protein and compl…

ChromatographybiologyChemistrymedicine.medical_treatmentSerum albuminProgesterone-Binding GlobulinDNA-binding proteinBlood proteinsSteroidSex hormone-binding globulinTranscortinAffinity chromatographybiology.proteinmedicine
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