Search results for "ovine"

showing 10 items of 317 documents

Inducing mixing of water-in water BSA/dextran emulsion by a strong polyelectrolyte

2015

Abstract We examine whether a small amount of strong polyelectrolyte (dextran sulfate sodium salt/DSS/) can induce mixing in water-in-water bovine serum albumin/dextran (BSA/DEX) emulsion and how intermacromolecular interactions affect its the rheological properties. Addition of DSS to water-in-water emulsion at pH 5.4 leads to its mixing at the DSS/BSA weight ratio, ( q ( DSS / BSA ) ) ≥ 0.07 , a noticeable increase in viscosity and storage modulus (G′). Mixing is reversible: increasing the ionic strength leads to phase separation in the water/BSA/DEX/DSS system. The increase in viscoelasticity results from the interaction of DSS with both macromolecular compounds of the emulsion. We assum…

Chromatographybiologyanimal diseasesGeneral Chemical EngineeringGeneral ChemistryCompatibilizationdigestive systemdigestive system diseasesPolyelectrolytecarbohydrates (lipids)stomatognathic diseaseschemistry.chemical_compoundDextranchemistryChemical engineeringIonic strengthEmulsionCopolymerbiology.proteinPolymer blendBovine serum albuminFood ScienceFood Hydrocolloids
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Evaluation of the proteolysis degree with the o-phthalaldehyde/N-acetyl-L-cysteine reagent

1990

The o-phthalaldehyde/N-acetyl-L-cysteine (OPA-NAC) reagent is applied to the spectrophotometric evaluation of the proteolytic activity of enzymes. The high stability of the OPA-NAC isoindoles makes a strict control of the time of reaction unnecessary. A mathematical expression is proposed to calculate proteolysis degrees, where the absorbance decrease of the OPA-NAC derivative of the protein itself during the hydrolysis process is taken into account. The method is applied to bovine serum albumine, caseine, lysozyme, lactoglobuline and protamine sulphate as substrates, and pronase, papaine, trypsin and chymotrypsin as enzymes.

ChymotrypsinChromatographybiologymedicine.diagnostic_testChemistryProteolysisPronaseTrypsinBiochemistryAnalytical ChemistryO-Phthalaldehydechemistry.chemical_compoundReagentbiology.proteinmedicineLysozymeBovine serum albuminmedicine.drugFresenius' Journal of Analytical Chemistry
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Irreversible formation of intermediate BSA oligomers requires and induces conformational changes.

2004

Understanding the relation between protein conformational changes and aggregation, and the physical mechanisms leading to such processes, is of primary importance, due to its direct relation to a vast class of severe pathologies. Growing evidence also suggests that oligomeric intermediates, which may occur early in the aggregation pathway, can be themselves pathogenic. The possible cytotoxicity of oligomers of non-disease-associated proteins adds generality to such suggestion and to the interest of studies of oligomer formation. Here we study the early stages of aggregation of Bovine Serum Albumin (BSA), a non pathogenic protein which has proved to be a useful model system. Dynamic light sc…

Circular dichroismAmyloidLightStereochemistryProtein ConformationProtein aggregationProcess interactionFibrilBiochemistryOligomerProtein Structure Secondarychemistry.chemical_compoundDynamic light scatteringStructural BiologyAnimalsScattering RadiationBovine serum albuminMolecular BiologybiologyCircular DichroismTemperatureSerum Albumin BovineKineticschemistrybiology.proteinCattleProteins
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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
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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
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The Interaction of Intravenous and Oral Biliary Contrast Agents with Serum Albumins

1978

The binding of two homologous series of oral and intravenous biliary contrast agents to human and bovine serum albumin was investigated using the gel filtration technique and circular dichroism measurements.

Circular dichroismChromatographybiologyChemistrymedia_common.quotation_subjectSize-exclusion chromatographyHuman serum albuminHomologous serieschemistry.chemical_compoundFlufenamic acidmedicinebiology.proteinContrast (vision)Bovine serum albuminmedicine.drugmedia_common
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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
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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
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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
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Anti-Listeria activity of citrus essential oils in a fresh ovine cheese

2023

The aim of this study was to evaluate the anti-Listeria activity of essential oils (EOs) extracted from the peel of lemons, oranges and tangerines in a fresh cheese produced with pasteurized ewe’s milk. Four cheesemaking trials were performed at the pilot plant scale level, including one control production without the addition of EOs and three experimental productions obtained by the addition of 200 μL/L of each EOs to milk. Before the addition of EOs, the milk of all trials was inoculated with 107 CFU/mL of the starter cultures (Lactococcus lactis NT1 and NT5) and 104 CFU/mL of pathogenic bacteria (Listeria monocytogenes ATCC19114). Plate counts confirmed the dominance of the starter cultu…

Citrus essential oilEwe’s milkSettore AGR/13 - Chimica AgrariaOvine cheese.Lactococcus lactiListeria monocytogeneSettore AGR/16 - Microbiologia Agraria
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