Search results for "bovine"

showing 10 items of 271 documents

Thermal Aggregation of Bovine Serum Albumin in Trehalose and Sucrose Aqueous Solutions

2012

We report results of static and dynamic light scattering measurements performed on bovine serum albumin (BSA) in saccharide (trehalose and sucrose) solutions. Our aim is to study the effects of the two disaccharides on the first steps of thermal aggregation of BSA in aqueous solutions at two protein concentrations (1 and 30 mg/mL) at increasing sugar/water ratio. Results show that sugars modify early stages of aggregation mainly by perturbing the thermodynamic behavior of the solvent (i.e., general solvent effects) without involving direct, specific sugar-protein interactions. This agrees with current hypotheses on sugar action in protein solutions. (1-3) The linear correlation detected bet…

SucroseSucrosechemistry.chemical_compoundDynamic light scatteringMaterials ChemistryAnimalsTransition TemperaturePhysical and Theoretical ChemistryBovine serum albuminProtein Structure QuaternarySugarChromatographyAqueous solutionbiologyTemperatureTrehaloseWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsSolutionsSolventtrehalose protein aggregation solvent effects light scatteringchemistrySolventsbiology.proteinCattleProtein MultimerizationSolvent effectsThe Journal of Physical Chemistry B
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The Influence of Hyaluronic Acid Biofunctionalization of a Bovine Bone Substitute on Osteoblast Activity In Vitro

2021

Bovine bone substitute materials (BSMs) are used for oral bone regeneration. The objective was to analyze the influence of BSM biofunctionalization via hyaluronic acid (HA) on human osteoblasts (HOBs). BSMs with ± HA were incubated with HOBs including HOBs alone as a negative control. On days 3, 7 and 10, cell viability, migration and proliferation were analyzed by fluorescence staining, scratch wound assay and MTT assay. On days 3, 7 and 10, an increased cell viability was demonstrated for BSM+ compared with BSM− and the control (each p ≤ 0.05). The cell migration was enhanced for BSM+ compared with BSM− and the control after day 3 and day 7 (each p ≤ 0.05). At day 10, an accelerated wound…

Technology02 engineering and technologyArticleAndrology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineHyaluronic acidhyaluronic acidmedicineGeneral Materials ScienceMTT assayViability assayxenograftoral regenerationBone regenerationMicroscopyQC120-168.85TbovineQH201-278.5biofunctionalizationosteoblastsOsteoblastCell migration030206 dentistrybone substituteEngineering (General). Civil engineering (General)021001 nanoscience & nanotechnologyIn vitroTK1-9971Bovine bonemedicine.anatomical_structureDescriptive and experimental mechanicschemistryElectrical engineering. Electronics. Nuclear engineeringTA1-20400210 nano-technologyMaterials
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Biodegradation of differently cross-linked collagen membranes: an experimental study in the rat.

2005

Contains fulltext : 47774.pdf (Publisher’s version ) (Closed access) The aim of the present study was to compare the biodegradation of differently cross-linked collagen membranes in rats. Five commercially available and three experimental membranes (VN) were included: (1) BioGide (BG) (non-cross-linked porcine type I and III collagens), (2) BioMend (BM), (3) BioMendExtend (BME) (glutaraldehyde cross-linked bovine type I collagen), (4) Ossix (OS) (enzymatic-cross-linked bovine type I collagen), (5) TutoDent (TD) (non-cross-linked bovine type I collagen, and (6-8) VN(1-3) (chemical cross-linked porcine type I and III collagens). Specimens were randomly allocated in unconnected subcutaneous po…

Tissue engineering and reconstructive surgery [UMCN 4.3]Time FactorsSwineForeign-Body ReactionBovine Type I CollagenTissue integrationCollagen membraneMembranes ArtificialAnatomyBiodegradationRatsAndrologychemistry.chemical_compoundMembranechemistryAbsorbable ImplantsAnimalsAnimal studyCattleGlutaraldehydeCollagenOral SurgeryRats Wistar
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Conformación tridimensional y reconocimiento molecular de biopolímeros : aplicación de RMN multidimensional y desarrollo de metodología de cálculo y …

1998

El objetivo principal de la Tesis ha sido la exploración, el análisis y el perfeccionamiento de las técnicas más habituales utilizadas en la determinación de la estructura y dinámica de biopolímeros en disolución. En concreto, se han utilizado métodos teóricos y experimentales para obtener las estructuras de dos biopolímeros entre los grupos más numerosos de ellos: proteínas y ácidos nucleicos. La obtención de la estructura de una proteína de interés bioquímico por sus peculiaridades cinéticas mediante dos técnicas diferentes ha sido uno de los objetivos principales en la Tesis. La aplicación de las técnicas de modelización por homología y la realización de un análisis exhaustivo sobre los …

UNESCO::CIENCIAS DE LA VIDA::Biofísica::Otrasbovine pancreatic trypsin inhibitorestructura de ácidos nucleicosprogramas de cálculoestructura de proteínas:CIENCIAS DE LA VIDA::Biofísica::Otras [UNESCO]UNESCO::QUÍMICA::Química física:QUÍMICA::Química física [UNESCO]plaastocianinaccgcggrmn
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Synthetic vaccines consisting of tumor-associated MUC1 glycopeptide antigens and bovine serum albumin.

2005

Vaccines SyntheticbiologyChemistryMolecular Sequence DataMucin-1Serum albuminGlycopeptidesSerum Albumin BovineStereoisomerismGeneral ChemistryCancer VaccinesCatalysisGlycopeptideBiochemistryAntigenCarbohydrate Sequencebiology.proteinCarbohydrate ConformationAnimalsHumansCattleCarbohydrate conformationBovine serum albuminMUC1Angewandte Chemie (International ed. in English)
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Synthetic vaccines of tumor-associated glycopeptide antigens by immune-compatible thioether linkage to bovine serum albumin.

2007

Vaccines SyntheticbiologyMolecular StructureGlycopeptidesSerum Albumin BovineGeneral ChemistrySulfidesCancer VaccinesCatalysisGlycopeptidechemistry.chemical_compoundImmune systemBiochemistryAntigenThioetherchemistryAntigens Neoplasmbiology.proteinAnimalsCattleBovine serum albuminAngewandte Chemie (International ed. in English)
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The foaming properties of camel and bovine whey: The impact of pH and heat treatment

2018

International audience; he effect of heat treatment (70 degrees C or 90 degrees C for 30 min) on the foaming and interfacial properties of acid and sweet whey obtained from bovine and camel fresh milk was examined. The maximum foamability and foam stability were observed for acid whey when compared to sweet whey for both milks, with higher values for the camel whey. This behavior for acid whey was explained by the proximity of the pI of whey protein (4.9-5.2), where proteins were found to carry the lowest negative charge as confirmed by the zeta potential measurements. Interfacial properties of acid camel whey and acid bovine whey were preserved at air water interface even after a heat trea…

Whey proteinHot TemperatureAir water interfaceCamel and bovine wheyAnalytical Chemistryfluids and secretions[SDV.IDA]Life Sciences [q-bio]/Food engineeringZeta potentialmixed layersFood scienceBeta-lactoglobulinbiologybeta-lactoglobulinChemistrypHdigestive oral and skin physiology[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringaggregationfood and beverages04 agricultural and veterinary sciencesGeneral MedicineHydrogen-Ion Concentration040401 food science[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]lactoferrinmilk-proteinsendocrine systemCamelusanimal structuresHeat treatmentinterfacesFresh milk0404 agricultural biotechnologyWheyNegative chargeFoaming propertiesalpha-lactalbuminAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]adsorption behaviorChromatographydromedarius milkViscoelastic modulus0402 animal and dairy sciencestability040201 dairy & animal scienceWhey ProteinsAlpha-lactalbuminbiology.proteinCattle[SDV.AEN]Life Sciences [q-bio]/Food and NutritionFood Science
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Effects of physico-chemical parameters of a model wine on the binding of γ-decalactone on bovine serum albumin

1995

Abstract To understand the effect of temperature, pH and the composition of alcoholic beverages in flavour-protein interactions, the binding of γ-decalactone to bovine serum albumin (BSA) was investigated using the equilibrium dialysis method. Thermodynamic analysis revealed that the affinity of aroma compound for BSA is higher at 10 °C than at 20 and 30 °C, while the number of binding sites (n = 6–7) is not modified at the three temperatures. pH did not have any appreciable effect on flavour binding in the presence of ethanol, but it was observed that a decrease of 1.8 pH unit reduces binding by 40% in its absence. The presence of ethanol has no effect on the number of binding sites and on…

WineEthanolChromatographybiologyAlbuminGeneral MedicineBinding constantAnalytical Chemistrychemistry.chemical_compoundchemistryIonic strengthbiology.proteinAroma compoundBinding siteBovine serum albuminFood ScienceFood Chemistry
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Flavour retention and release from protein solutions

2006

International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyPROTEINSFlavourBioengineeringLactoglobulins01 natural sciencesApplied Microbiology and Biotechnology0404 agricultural biotechnologyComputational chemistryCyclohexenesHumansBinding siteAromaStrong bindingFlavorBinding SitesbiologyFLAVOUR RELEASETerpenesChemistry010401 analytical chemistryBinding propertiesfood and beveragesSerum Albumin Bovine04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationMilk Proteinsbiology.organism_classification040401 food science0104 chemical sciences[SDV.BIO] Life Sciences [q-bio]/BiotechnologyFlavoring AgentsBiochemistryBenzaldehydesTasteFLAVOUR BINDINGSoybean ProteinsFood TechnologyLimoneneProtein BindingBiotechnology
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Fast detection of bovine milk in Rocquefort cheese with phastsystem by gel isoelectric focusing and immunoblotting

1992

.Summary - A fast procedure for the detection of bovine milk in Roquefort cheese is described. It is based on the separation by rapid isoelectric focusing on Phasteysterne apparatus of 12-caseinsfrom the milk of the 2 species. The presence of bovine milk is also confirmed by the detection in the electrophoretic pattern of a ~-casein derived peptide from bovine milk, during cheese ripening, identified by immunoblotting. By using Ihis procedure, levels of bovine milk as low as 5% were easily delecled in Roquefort cheese ripened for a period varying from 10 days to 5 months.

[SDV.SA]Life Sciences [q-bio]/Agricultural sciencesBovine milkRoquefort cheeseBlue cheeseCheese ripeningBiology01 natural sciencesCow milkfluids and secretionsfoodCaseinFood sciencefood.cheeseComputingMilieux_MISCELLANEOUS[SDV.SA] Life Sciences [q-bio]/Agricultural sciencesChromatographyIsoelectric focusing010401 analytical chemistry0402 animal and dairy sciencefood and beverages04 agricultural and veterinary sciences[SDV.IDA] Life Sciences [q-bio]/Food engineering040201 dairy & animal science0104 chemical sciences[SDV.AEN] Life Sciences [q-bio]/Food and NutritionFood Science
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