Search results for " bovine"

showing 10 items of 151 documents

Role of Seroalbumin in the Cytotoxicity of cis-Dichloro Pt(II) Complexes with (N^N)-Donor Ligands Bearing Functionalized Tails

2018

Given the potent anticancer properties of cisdiamminedichloroplatinum( II) and knowing its mode of action, we synthesized four new cis-[PtCl2(N^N)] organoplatinum complexes, two with N-substituted pbi ligands (pbiR = 1-R-2-(2-pyridyl)benzimidazole) (namely, 1 and 2) and two more with 4,4′-disubstituted bpy ligands (bpy = 2,2′-bipyridine) (namely, 3 and 4). We explored their cytotoxicity and ability to bind to deoxyguanosine monophosphate (dGMP), DNA, and albumin models. By 1H NMR and UV−vis spectroscopies, circular dichroism, agarose gel electrophoresis, differential scanning calorimetry measurements, and density functional theory calculations, we verified that only 3 can form aquacomplex s…

Circular dichroismCell SurvivalStereochemistryLigandPlasma protein bindingHeLa CellLigands010402 general chemistry01 natural sciencesChemistry Physical and theoreticalInorganic ChemistryHeLaBipyridinechemistry.chemical_compoundDrug StabilityCoordination ComplexesQuímica físicaHumansPhysical and Theoretical ChemistryCytotoxicityA549 CellOrganoplatinumPlatinumCoordination ComplexeCalorimetry Differential ScanningMolecular Structurebiology010405 organic chemistryChemistryRational designDeoxyguanine NucleotidesSerum Albumin BovineDNAbiology.organism_classification0104 chemical sciencesSettore CHIM/03 - Chimica Generale E InorganicaA549 CellsAgarose gel electrophoresisDeoxyguanine NucleotideHumanHeLa CellsProtein BindingInorganic Chemistry
researchProduct

Optical studies on interaction of biliary contrast agents with native and modified human serum albumin.

1981

The interaction of two homologous series of biliary contrast agents with native human and bovine serum albumin and with modified human serum albumin was investigated using circular dichroism and equilibrium dialysis. For most derivatives, extrinsic Cotton effects were observed for the interaction with both albumins. In some cases, these effects were strongly affected by only small changes in the chemical structure of the drugs. These large differences in extrinsic Cotton effects can be explained by definite effects of the chemical structures on the binding site selectivity of some drugs. For example, iopodate preferentially binds to the warfarin binding site of human Scrum albumin, while an…

Circular dichroismChemical PhenomenaSerum albuminPharmaceutical ScienceContrast MediaPlasma protein bindingmedicineAnimalsHumansBovine serum albuminBinding siteBiliary TractSerum AlbuminDiazepam bindingbiologyChemistryCircular DichroismAlbuminTryptophanSerum Albumin BovineHuman serum albuminRadiographyChemistryBiochemistrybiology.proteinTyrosineCattleDialysismedicine.drugProtein BindingJournal of pharmaceutical sciences
researchProduct

Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

2011

We report an experimental study on the model protein Bovine Serum Albumin (BSA), with the aim of elucidating the mechanisms by which a fully folded globular protein undergoes different aggregation pathways leading to the formation of amyloid fibrils or amorphous aggregates. We observe thermally induced formation of fibrillar structures at pH far from the protein isoelectric point. The increase of electrostatic repulsion results in protein destabilization and in modifications of inter and intra-molecular interactions leading to the growth of fibril-like aggregates stabilized by inter-molecular-β sheets. The aggregation kinetics is studied by means of fluorescence techniques, light scattering…

Circular dichroismProtein ConformationGlobular proteinStatic ElectricityBiophysicsProtein aggregationBiochemistryprotein aggregation amyloid fibril fluorescence conformational changeschemistry.chemical_compoundProtein structureAnimalsBenzothiazolesBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologyTemperatureTryptophanSerum Albumin BovineHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsThiazolesCrystallographyIsoelectric pointchemistryProtein destabilizationbiology.proteinThermodynamicsCattleThioflavinProtein Multimerization
researchProduct

Calorimetric and structural investigation of the interaction between bovine serum albumin and high molecular weight dextran in water.

2005

This work studies specific interactions between a small globular protein and a highly flexible, branched polysaccharide using differential scanning calorimetry (DSC), circular dichroism (CD), fluorescence, and turbidimetry measurements. It uses the system water/bovine serum albumin (BSA)/dextran (D 2000) as a model. Dextran molecules are able to form interpolymeric complexes with BSA in water at both low and high temperatures if the polysaccharide is in excess and if the protein exists in its associated state. It leads to a partial destabilization of the secondary and tertiary structures of the protein and an additional exposure of the hydrophobic tryptophan residues to the surface of globu…

Circular dichroismProtein DenaturationProtein FoldingPolymers and PlasticsGlobular proteinMacromolecular SubstancesPolymersProtein ConformationUltraviolet RaysSerum albuminBioengineeringBiocompatible MaterialsCalorimetryProtein Structure SecondaryBiomaterialschemistry.chemical_compoundProtein structureNephelometry and TurbidimetryPolysaccharidesMaterials TestingMaterials ChemistryAnimalsBovine serum albuminchemistry.chemical_classificationChromatographybiologyCalorimetry Differential ScanningChemistryCircular DichroismTemperatureWaterDextransSerum Albumin BovineProtein Structure TertiaryDextranSpectrometry FluorescenceCalibrationbiology.proteinThermodynamicsProtein foldingCattleTurbidimetryBiomacromolecules
researchProduct

Thermal aggregation and ion-induced cold-gelation of bovine serum albumin

2009

Protein cold-gelation has recently received particular attention for its relevance in bio and food technology. In this work, we report a study on bovine serum albumin cold-gelation induced by copper or zinc ions. Metal-induced cold-gelation of proteins requires two steps: during the first one, the heat treatment causes protein partial unfolding and aggregation; then, after cooling the solution to room temperature, gels are formed upon the addition of metal ions. The thermally induced behaviour has been mainly investigated through different techniques: Fourier transform infrared (FTIR) spectroscopy, circular dichroism, dynamic light scattering (DLS) and rheology. Data have shown that the agg…

Circular dichroismProtein FoldingTime FactorsLightMetal ions in aqueous solutionBiophysicsAnalytical chemistryViscoelasticityProtein Structure SecondaryIonDivalentDynamic light scatteringSpectroscopy Fourier Transform InfraredAnimalsScattering RadiationBovine serum albuminFourier transform infrared spectroscopychemistry.chemical_classificationbiologyChemistryCircular DichroismTemperatureSerum Albumin BovineGeneral MedicineElasticityKineticsZincbiology.proteinCattleRheologyCopperBovine serum albumin (BSA)Proteins aggregation Metal ions Cold-gelation
researchProduct

Prenatal Diagnosis of Bovine Aortic Arch Anatomic Variant

2022

Fetal aortic arch development is an early and complex process that depends on many genetic and environmental factors. The final aortic arch varies greatly; it may take the form of a normal arch, anatomic variant (AAAV) with a common origin to that of the innominate artery and left common carotid artery (formerly known as “bovine aortic arch” (with an incidence of up to 27%)) or one of multiple pathological conditions. The present study aimed to establish the feasibility and impact of prenatal anatomic arch variants’ diagnosis. A retrospective study of 271 fetal second- and third-trimester anomaly scans was performed in our tertiary center. Examinations that evaluated the s…

Clinical Biochemistryaortic arch variant; bovine aortic arch; prenatal diagnosis; cardiac surgeryDiagnostics
researchProduct

Phase behavior of aqueous solutions of bovine serum albumin in the presence of dextran, at rest, and under shear.

2006

The demixing conditions for aqueous solutions of bovine serum albumin (BSA, fraction V) and for joint solutions of BSA plus dextran (DEX, M(w) = 2000 kg/mol) were determined by turbidimetric measurements as a function of composition, temperature, and shear rate. Aqueous solutions of BSA phase separate upon heating. Within the region of BSA concentrations between 0.05 and 32 wt %, the demixing temperature, T1, falls from ca. 65 degrees C to an almost constant value of 45 degrees C. Adding DEX to the BSA solutions reduces the homogeneous region of the mixture drastically where the amount of DEX required to lower T1 to 25 degrees C decreases rapidly as the concentration of BSA is raised. Exper…

Cloud pointAqueous solutionChromatographyTernary numeral systemPolymers and PlasticsbiologySerum albuminWaterBioengineeringDextransSerum Albumin BovineBiomaterialsShear rateSolutionschemistry.chemical_compoundDextranchemistryNephelometry and TurbidimetryPhase (matter)Materials Chemistrybiology.proteinThermodynamicsStress MechanicalBovine serum albuminBiomacromolecules
researchProduct

Inhibition of DNA synthesis in chick embryo retinas, in vitro, by a factor from fetal bovine serum

1989

Fetal bovine serum inhibited deoxyribonucleic acid (DNA) synthesis in chick embryo retina explants. The inhibitory activity was precipitated from fetal bovine serum by 45% saturated ammonium sulfate and isolated by means of Sephadex G-100 and Bio-Gel P-60 columns as a peak with an apparent molecular weight of 7000 Da. DNA-inhibiting activity was heat- and acid-stable and was destroyed by dithiothreitol and alkaline treatment. The purified factor inhibited similarly both DNA synthesis and thymidine kinase activity; 50% inhibitory effect was found with 160 ng, 17 h after the addition into the incubation medium.

DNA ReplicationThymidine kinase activityDNA synthesisEmbryoBlood ProteinsBiologyMolecular biologyGrowth InhibitorsRetinaIn vitroDithiothreitolMolecular Weightchemistry.chemical_compoundOrgan Culture TechniquesDevelopmental NeurosciencechemistryBiochemistrySephadexAnimalsCattlechick embryoFetal bovine serumDNADevelopmental BiologyDevelopmental Brain Research
researchProduct

Methicillin-resistant Staphylococcus pseudintermedius as causative agent of dairy cow mastitis.

2013

Staphylococcus pseudintermedius is a coagulase-positive specie similar to Staphylococcus intermedius , frequently associated with pyoderma, otitis and urinary tract infections of dogs and cats (van Duijkeren and others 2011). No information about bovine mastitis caused by S pseudintermedius is available in the literature. Antimicrobial resistance among S pseudintermedius strains is increasing: in the past, susceptibility to most antibiotics was common (Bond and Loeffler 2012), but in the last few years methicillin-resistant S pseudintermedius (MRSP) strains have emerged as a significant animal health problem in veterinary medicine (Schwarz and others 2008, van Duijkeren and others 2008, Wee…

DNA BacterialSettore MED/07 - Microbiologia E Microbiologia ClinicaVeterinary medicineStaphylococcus pseudintermediusStaphylococcusPyodermaMicrobial Sensitivity Testsmedicine.disease_causeMicrobiologyMicrobiologyAntibiotic resistancemedicinePrevalenceDairy cattleAnimalsMastitis BovineBacteriological TechniquesMastitiGeneral VeterinarybiologyStaphylococcus intermediusbusiness.industrySCCmecGeneral MedicineStaphylococcal Infectionsbiology.organism_classificationmedicine.diseaseMastitisStaphylococcus aureusHerdCattleFemaleMethicillin ResistancebusinessThe Veterinary record
researchProduct

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
researchProduct