Search results for "Cattle"

showing 10 items of 608 documents

Localization of the N-terminal Domain in Light-harvesting Chlorophyll a/b Protein by EPR Measurements

2005

The conformational distribution of the N-terminal domain of the major light-harvesting chlorophyll a/b protein (LHCIIb) has been characterized by electron-electron double resonance yielding distances between spin labels placed in various domains of the protein. Distance distributions involving residue 3 near the N terminus turned out to be bimodal, revealing that this domain, which is involved in regulatory functions such as balancing the energy flow through photosystems (PS) I and II, exists in at least two conformational states. Models of the conformational sub-ensembles were generated on the basis of experimental distance restraints from measurements on LHCIIb monomers and then checked f…

ChlorophyllModels MolecularThreonineConformational changeTime FactorsLightMacromolecular SubstancesProtein ConformationPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesElectronsTrimerCrystallography X-RayThylakoidsBiochemistryProtein Structure Secondarylaw.inventionResidue (chemistry)chemistry.chemical_compoundlawEscherichia coliAnimalsPhosphorylationAnnexin A4Electron paramagnetic resonanceMolecular BiologyPhotosystemPhotosystem I Protein ComplexChemistryChlorophyll AElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsProtein Structure TertiaryOxygenN-terminusCrystallographyMonomerThylakoidMutationCattleSpin LabelsDimerizationJournal of Biological Chemistry
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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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Extraction of clenbuterol from calf urine using a molecularly imprinted polymer followed by quantitation by high-performance liquid chromatography wi…

2002

A method for the extraction of clenbuterol from calf urine samples using a molecularly imprinted polymer (MIP) has been developed. The aim was that the final extracts from the MIP should allow quantitation of clenbuterol down to 0.5 ng/mL urine using HPLC with UV detection. The MIP was produced using brombuterol as a template and the selectivity of the MIP, for clenbuterol, was tested against a non-imprinted polymer (produced without template) and was found to be high. After loading of 5 mL diluted centrifuged urine, selective binding was established in acetonitrile-acetic acid (98:2). For further elution of interferences, 0.5 M ammonium acetate buffer pH 5 and 70% acetonitrile in water was…

ChromatographyChemistryElutionOrganic ChemistryExtraction (chemistry)Molecularly imprinted polymerReproducibility of ResultsGeneral MedicineReversed-phase chromatographyReference StandardsSensitivity and SpecificityBiochemistryHigh-performance liquid chromatographyAnalytical ChemistryClenbuterolmedicineAnimalsCattleClenbuterolSpectrophotometry UltravioletSample preparationSolid phase extractionAdrenergic alpha-AgonistsChromatography High Pressure Liquidmedicine.drugJournal of Chromatography A
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High-performance liquid chromatographic determination of Maillard compounds in store-brand and name-brand ultra-high-temperature-treated cows' milk.

2000

Furosine and furfural products of the Maillard reaction are used as specific indicators of the effect of heating treatments on milk quality. Their contents were measured in representative samples of store- and name-brand ultra-high-temperature-treated milks using RP-HPLC with UV detection. Furosine contents ranged from 40.32 to 50.67 and from 65.48 to 310.58 mg/100 g protein in name- and store-brand milks, respectively. Of the furfurals, only hydroxymethylfurfural was detected. The free hydroxymethylfurfural contents of store-brand milks ranged from 0.22 to 1.70 mg/100 g protein. Total hydroxymethylfurfural contents ranged from 0.29 to 0.41 and from 0.72 to 2.21 mg/100 g protein, for name- …

ChromatographyHot TemperatureOrganic ChemistryFood composition dataGeneral MedicineReversed-phase chromatographyFurfuralBiochemistryHigh-performance liquid chromatographyAnalytical ChemistryMaillard Reactionchemistry.chemical_compoundMaillard reactionsymbols.namesakeMilkchemistrysymbolsAnimalsCattleSpectrophotometry UltravioletUv detectionQuantitative analysis (chemistry)HydroxymethylfurfuralChromatography High Pressure LiquidJournal of chromatography. A
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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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Halloysite nanotubes-carbon dots hybrids multifunctional nanocarrier with positive cell target ability as a potential non-viral vector for oral gene …

2019

Abstract Hypothesis The use of non-viral vectors for gene therapy is hindered by their lower transfection efficiency and their lacking of self-track ability. Experiments This study aims to investigate the biological properties of halloysite nanotubes-carbon dots hybrid and its potential use as non-viral vector for oral gene therapy. The morphology and the chemical composition of the halloysite hybrid were investigated by means of high angle annular dark field scanning TEM and electron energy loss spectroscopy techniques, respectively. The cytotoxicity and the antioxidant activity were investigated by standard methods (MTS, DPPH and H2O2, respectively) using human cervical cancer HeLa cells …

Circular dichroismCell SurvivalSurface PropertiesStatic ElectricityAdministration Oral02 engineering and technologyCellular imagingengineering.material010402 general chemistry01 natural sciencesHalloysiteAntioxidantsBiomaterialsHeLaColloid and Surface ChemistryDynamic light scatteringFluorescence microscopeTumor Cells CulturedCarbon dotsAnimalsHumansParticle SizeSettore CHIM/02 - Chimica FisicaDrug CarriersbiologyMolecular StructureHalloysite nanotubesChemistryNanotubes CarbonOptical ImagingGene Transfer TechniquesTransfectionDNASettore CHIM/06 - Chimica Organica021001 nanoscience & nanotechnologybiology.organism_classificationDark field microscopyDNA interaction0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsHalloysite nanotubes Carbon dots DNA interaction Cellular imagingengineeringBiophysicsCattleNanocarriers0210 nano-technologyPorosityHeLa Cells
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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 native DNA with iron(III)- N ,N'-ethylene-bis(salicylideneiminato)-chloride.

2004

Abstract The interaction between native calf thymus deoxyribonucleic acid (DNA) and Fe III - N , N ′ -ethylene-bis (salicylideneiminato)-chloride, Fe(Salen)Cl, was investigated in aqueous solutions by UV–visible (UV–vis) absorption, circular dichroism (CD), thermal denaturation and viscosity measurements. The results obtained from CD, UV–vis and viscosity measurements exclude DNA intercalation and can be interpreted in terms of an electrostatic binding between the Fe(Salen) + cation and the phosphate groups of DNA. The trend of the UV–vis absorption band of the Fe(Salen)Cl complex at different ratios [DNA phosphate ]/[Fe(Salen)Cl] and the large increase of the melting temperature of DNA in …

Circular dichroismInorganic chemistryNucleic Acid DenaturationBiochemistryChlorideFerric CompoundsInorganic Chemistrychemistry.chemical_compoundMetal salen complexesmedicineAnimalsSchiff BasesAqueous solutionChemistryViscosityCircular DichroismSpectrum AnalysisDNAIron IsotopesCrystallographyDNA IntercalationAbsorption bandCattleAbsorption (chemistry)DNAmedicine.drugJournal of inorganic biochemistry
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The interaction of native DNA with Zn(II) and Cu(II) complexes of 5-triethyl ammonium methyl salicylidene orto-phenylendiimine

2007

The interaction of native calf thymus DNA with the Zn(II) and Cu(II) complexes of 5-triethyl ammonium methyl salicylidene orto-phenylendiimine (ZnL(2+) and CuL(2+)), in 1 mM Tris-HCl aqueous solutions at neutral pH, has been monitored as a function of the metal complex-DNA molar ratio by UV absorption spectrophotometry, circular dichroism (CD) and fluorescence spectroscopy. The results support for an intercalative interaction of both ZnL(2+) and CuL(2+) with DNA, showing CuL(2+) an affinity of approximately 10 times higher than ZnL(2+). In particular, the values of the binding constant, determined by UV spectrophotometric titration, equal to 7.3x10(4) and 1.3x10(6)M(-1), for ZnL(2+) and CuL…

Circular dichroismInorganic chemistrychemistry.chemical_elementZincNucleic Acid DenaturationBiochemistryFluorescence spectroscopyInorganic ChemistryMetalSchiff baseOrganometallic CompoundsIntercalationAnimalsQualitative inorganic analysisSchiff BasesAqueous solutionQuenching (fluorescence)ChemistryCircular DichroismDNASettore CHIM/06 - Chimica OrganicaBinding constantQuaternary Ammonium CompoundsCrystallographyZincSettore CHIM/03 - Chimica Generale E Inorganicavisual_artvisual_art.visual_art_mediumCattleSpectrophotometry UltravioletIminesCopper
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Confinement effects on the interactions of native DNA with Cu(II)-5-triethyl ammonium methyl salicylidene orto-phenylendiiminate in C12E4 liquid crys…

2008

Confinement effects of native calf thymus DNA interacting with the complex Cu(ii)-5-(triethylammoniummethyl)salicylidene ortho-phenylendiiminate (CuL(2+)) perchlorate in tetraethylene glycol monododecyl ether (C(12)E(4)) liquid crystals have been investigated by UV absorption spectrophotometry, circular dichroism (CD) and small angle X-ray scattering (SAXS). The results indicate the occurrence of dramatic structural changes of both the DNA and the CuL(2+)-DNA system, when going from aqueous solution to C(12)E(4) liquid crystals, due to confinement constrains imposed by the closed structure of C(12)E(4) reverse micelles. Further marked departures from the behaviour observed in aqueous soluti…

Circular dichroismIntracellular SpaceMicelleAbsorptionPolyethylene GlycolsInorganic ChemistryPerchloratechemistry.chemical_compoundX-Ray DiffractionLiquid crystalScattering Small AngleOrganometallic CompoundsAnimalsSettore CHIM/02 - Chimica FisicaAqueous solutionSmall-angle X-ray scatteringCircular DichroismWaterDNALiquid CrystalsCrystallographychemistrySettore CHIM/03 - Chimica Generale E InorganicaX-ray crystallographyCattleSpectrophotometry UltravioletAbsorption (chemistry)DNA intercalation reverse micelles
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