Search results for "Cattle"

showing 10 items of 608 documents

Synthesis of pyrido[2,1-a]isoquinolin-4-ones and oxazino[2,3-a]isoquinolin-4-ones: New inhibitors of mitochondrial respiratory chain

2013

International audience; Benzo[a]quinolizine is an important heterocyclic framework that can be found in numerous bioactive compounds. The general scheme for the synthesis of these compounds was based on the preparation of the appropriate dihydroisoquinolines by Bischler-Napieralski cyclization with good yields, followed by the Pemberton method to form the oxazinones or pyridones derivatives via acyl-ketene imine cyclocondensation. All the synthesized compounds were assayed in vitro for their ability to inhibit mitochondrial respiratory chain. Most of the tested compounds were able to inhibit the integrated electron transfer chain, measured as NADH oxidation, which includes complexes I, III …

PyridonesStereochemistryImine010402 general chemistryRing (chemistry)01 natural sciencesMitochondria HeartElectron TransportStructure-Activity Relationshipchemistry.chemical_compoundMultienzyme ComplexesFuranOxazinesDrug DiscoveryAnimalsNADH NADPH OxidoreductasesCytotoxicityPharmacologyDose-Response Relationship DrugMolecular Structure[CHIM.ORGA]Chemical Sciences/Organic chemistry010405 organic chemistryOrganic ChemistryQuinolizineBiological activityGeneral MedicineIsoquinolinesElectron transport chain3. Good health0104 chemical sciencesMitochondrial respiratory chainchemistryCattleEuropean Journal of Medicinal Chemistry
researchProduct

Surface-Enhanced Raman Study of the Interactions between Tripodal Cationic Polyamines and Polynucleotides

2011

Raman and surface-enhanced Raman spectra of new DNA/RNA-binding compounds consisting of three imidazole (Im) and three pyridine (Py) rings connected by tripodal polyaminomethylene linkages were obtained by the near-infrared excitation at 1064 nm. Study of interactions of Im and Py polyamines with single-stranded RNA polynucleotides (poly A, poly G, poly C, poly U), double-stranded DNA polynucleotides (poly dAdT-poly dAdT, poly dGdC-poly dGdC) and calf thymus DNA (ct-DNA) by surface-enhanced Raman spectroscopy (SERS) reveals unambiguous enhancement of the Raman scattering from the small molecules as well as appearance of new bands in spectra associated mainly with nucleobases. The SERS exper…

PyrimidinePyridinesStereochemistryGuaninePolynucleotidesSpectrum Analysis RamanBiochemistryAnalytical ChemistryNucleobasechemistry.chemical_compoundsymbols.namesakePolyaminesElectrochemistryAnimalsEnvironmental ChemistryImidazoleSpectroscopyImidazolesAromaticityDNAsurface-enhanced Raman spectroscopy ; polyamines ; polynucleotides ; DNAchemistryPolynucleotidesymbolsRNACattleRaman spectroscopyDNA
researchProduct

Uptake of silica covered Quantum Dots into living cells: Long term vitality and morphology study on hyaluronic acid biomaterials

2015

Quantum Dots (QDs) are promising very bright and stable fluorescent probes for optical studies in the biological field but water solubility and possible metal bio-contamination need to be addressed. In this work, a simple silica-QD hybrid system is prepared and the uptake in bovine chondrocytes living cells without any functionalization of the external protective silica shield is demonstrated. Moreover, long term treated cells vitality (up to 14 days) and the transfer of silica-QDs to the next cell generations are here reported. Confocal fluorescence microscopy was also used to determine the morphology of the so labelled cells and the relative silica-QDs distribution. Finally, we employ sil…

Quantum DotNanoparticleBiocompatible Materials02 engineering and technology01 natural scienceschemistry.chemical_compoundNanoparticleLabellingHyaluronic acidFluorescence microscopeLong term cell stainingBiocompatible MaterialSilicon Dioxide021001 nanoscience & nanotechnologyMechanics of MaterialsSelf-healing hydrogelsMaterials Science (all)0210 nano-technologySilica Quantum DotMaterials scienceFluorescence confocal microscopyCell SurvivalSilicon dioxideChondrocyte bovine cellHyaluronic acidConfocalBioengineeringNanotechnologyCondensed Matter Physic010402 general chemistryBiomaterialsChondrocytesQuantum DotsAnimalsMechanics of MaterialCell ShapeSilica Quantum DotsAnimalMechanical Engineeringtechnology industry and agricultureChondrocyteequipment and suppliesSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesMicroscopy FluorescencechemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoQuantum dotBiophysicsNanoparticlesSurface modificationCattleMaterials Science and Engineering: C
researchProduct

Iodine determination in food samples using inductively coupled plasma isotope dilution mass spectrometry.

1998

Two different sample treatment methods are used in connection with inductively coupled plasma isotope dilution mass spectrometry for accurate and precise determinations of iodine traces in food samples. 129I-enriched iodate is applied as a spike compound for the isotope dilution step. Extraction of iodine by tetramethylammonium hydroxide (TMAH) solution at high temperatures in a closed vessel is one of the sample treatment methods. The other one is a complete decomposition of the sample with a mixture of perchloric acid and nitric acid using microwave assistance. By analyzing different certified reference materials (three milk powders with different iodine levels, BCR CRM 63, 150, and 151; …

Radioisotope Dilution TechniqueAnalytical chemistryIodateschemistry.chemical_elementIsotope dilutionIodineMass spectrometryNitric AcidMass SpectrometryAnalytical ChemistryIodine Radioisotopeschemistry.chemical_compoundAnimalsHumansMicrowavesIodateDetection limitChromatographyPerchloratesChemistryInfant NewbornReproducibility of ResultsIodine RadioisotopesQuaternary Ammonium CompoundsCertified reference materialsMilkLiverCattleInfant FoodDairy ProductsInductively coupled plasmaIodineAnalytical chemistry
researchProduct

Species- and Subtype-Specific Recognition by Antibody WF6 of a Sequence Segment Forming an α-Bungarotoxin Binding Site on the Nicotinic Acetylcholine…

1992

The monoclonal antibody WF6 competes with acetylcholine and alpha-bungarotoxin (alpha-BGT) for binding to the Torpedo nicotinic acetylcholine receptor (nAChR) alpha 1 subunit. Using synthetic peptides corresponding to the complete Torpedo nAChR alpha 1 subunit, we previously mapped a continuous epitope recognized by WF6, and the prototope for alpha-BGT, to the sequence segment alpha 1(181-200). Single amino acid substitution analogs have been used as an initial approach to determine the critical amino acids for WF6 and alpha-BGT binding. In the present study, we continue our analysis of the structural features of the WF6 epitope by comparing its cross-reactivity with synthetic peptides corr…

Ranidaealpha7 Nicotinic Acetylcholine ReceptorMolecular Sequence DataCross ReactionsReceptors NicotinicBiologyTorpedoEpitopelaw.inventionMiceSpecies SpecificityAntibody SpecificitylawSequence Homology Nucleic AcidmedicineAnimalsHumansReceptors CholinergicAmino Acid SequenceBinding sitePharmacologyMusclesBinding proteinAntibodies MonoclonalSnakesBungarotoxinsMolecular biologyRatsNicotinic acetylcholine receptorBiochemistryCattleAlpha-4 beta-2 nicotinic receptorPeptidesTorpedoAcetylcholineCys-loop receptorsmedicine.drugJournal of Receptor Research
researchProduct

1-Methyl-?-carboline (Harmane), a potent endogenous inhibitor of benzodiazepine receptor binding

1980

The interaction of several beta-carbolines with specific [3H]-flunitrazepam binding to benzodiazepine receptors in rat brain membranes was investigated. Out of the investigated compounds, harmane and norharmane were the most potent inhibitors of specific [3H]-flunitrazepam binding, with IC50-values in the micromolar range. All other derivatives, including harmine, harmaline, and several tetrahydroderivatives were at least ten times less potent. Harmane has been previously found in rat brain and human urine, so it is the most potent endogenous inhibitor of specific [3H]-flunitrazepam binding known so far, with a several fold higher affinity for the benzodiazepine receptor than inosine and hy…

Receptors DrugFlunitrazepamIn Vitro TechniquesPharmacologyRetinachemistry.chemical_compoundHarmalineAlkaloidsHarminemedicineAnimalsHarmaneInosineBenzodiazepine receptor bindingBrain ChemistryPharmacologybeta-CarbolineGABAA receptormusculoskeletal neural and ocular physiologyGeneral MedicineReceptors GABA-ARatsHarmineKineticschemistryBiochemistryCattleFlunitrazepammedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
researchProduct

Production of biologically active light chain of tetanus toxin inEscherichia coli

1993

AbstractThe activity of the light (L) chain of tetanus toxin, and of mutants constructed by site-directed mutagenesis, was studied by expression and purification of the proteins from E. coli. Wild-type recombinant L chain (pTet87) was active in the inhibition of exocytosis from cultured bovine adrenal chromaffin cells, although at a level 5–15% of that of L chain purified from tetanus toxin. L chain mutants which terminated at Leu-438 (pTet89), or which contained a Cys-to-Ser mutation at residue 439 (pTet88) were equally as active as the full-length recombinant protein. The reduced activity of pTet87 L chain correlated with C-terminal proteolysis of the protein upon purification. A tryptic …

Recombinant proteinMacromolecular SubstancesProteolysisMolecular Sequence DataRestriction MappingDNA RecombinantBiophysicsBiologymedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosislaw.inventionNorepinephrineTetanus ToxinStructural BiologylawEscherichia coliGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularSite-directed mutagenesisMolecular BiologyEscherichia coliCells Culturedchemistry.chemical_classificationBase Sequencemedicine.diagnostic_testToxinBiological activityCell BiologyMolecular biologyRecombinant ProteinsE. coli Chromaffin cellAmino acidKineticsOligodeoxyribonucleotideschemistryBiochemistryAdrenal MedullaMutagenesis Site-DirectedRecombinant DNACalciumCattleElectrophoresis Polyacrylamide GelSite directed mutagenesisFEBS Letters
researchProduct

NMR relaxation times of trabecular bone—reproducibility, relationships to tissue structure and effects of sample freezing

2010

Nuclear magnetic resonance (NMR) spectroscopy provides a potential tool for non-invasive evaluation of the trabecular bone structure. The objective of this study was to determine the reproducibility of the NMR relaxation parameters (T(2), Carr-Purcel-T(2), T(1ρ)) for fat and water and relate those to the structural parameters obtained by micro-computed tomography (μCT). Especially, we aimed to evaluate the effect of freezing on the relaxation parameters. For storing bone samples, freezing is the standard procedure during which the biochemical and cellular organization of the bone marrow may be affected. Bovine trabecular bone samples were stored at -20 °C for 7 days and measured by NMR spec…

ReproducibilityMagnetic Resonance SpectroscopyTime FactorsRotationTibiaRadiological and Ultrasound TechnologyChemistryCoefficient of variationRelaxation (NMR)Reproducibility of ResultsWaterX-Ray MicrotomographyNuclear magnetic resonance spectroscopyTrabecular boneNuclear magnetic resonancemedicine.anatomical_structureAdipose TissueRelaxation rateFreezingmedicineAnimalsCattleRadiology Nuclear Medicine and imagingBone marrowSpectroscopyPhysics in Medicine and Biology
researchProduct

Rhodopsin transport in the membrane of the connecting cilium of mammalian photoreceptor cells

2000

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study was to resolve rhodopsin trafficking from the inner to the outer segment. We demonstrate, predominantly by high-sensitive immunoelectron microscopy, that rhodopsin is also densely packed in the membrane of the photoreceptor connecting cilium. Present prominent labeling of rhodopsin in the ciliary mem…

RhodopsinOpsingenetic structuresPhotoreceptor Connecting CiliumImmunoblottingMolecular Sequence Datamacromolecular substancesMyosinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceRetinal Rod Photoreceptor CellsStructural BiologymedicineAnimalsHumansPhotopigmentAmino Acid SequenceCiliaMicroscopy ImmunoelectronCiliary membraneCiliumRod OpsinsAntibodies MonoclonalDyneinsBiological TransportCell BiologyMiddle AgedRod Cell Outer SegmentActin cytoskeletonImmunohistochemistryActinseye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureRhodopsinMyosin VIIabiology.proteinCattleFemalesense organsRetinitis PigmentosaCell Motility and the Cytoskeleton
researchProduct

Differential expression and interaction with the visual G-protein transducin of centrin isoforms in mammalian photoreceptor cells.

2004

Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells. Massive translocation of the visual G-protein transducin, Gt, between subcellular compartments contributes to long term adaptation of photoreceptor cells. Ca(2+)-triggered assembly of a centrin-transducin complex in the connecting cilium of photoreceptor cells may regulate these transducin translocations. Here we demonstrate expression of all four known, closely related centrin isoforms in the mammalian retina. Interaction assays revealed binding potential of the four centrin isoforms to Gtbetagamma heterodimers. High affinity b…

Rhodopsingenetic structuresLightBlotting WesternBiologyBiochemistryRetinaRats Sprague-DawleyMiceCalcium-binding proteinHeterotrimeric G proteinmedicineAnimalsProtein IsoformsScattering RadiationCiliaTransducinMicroscopy ImmunoelectronMolecular BiologyCyclic GMPGlutathione TransferaseCentrosomeRetinaChromatographyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionCiliumCalcium-Binding ProteinsCell BiologySequence Analysis DNARod Cell Outer SegmentRecombinant ProteinsCell biologyRatsMice Inbred C57BLKineticsProtein Transportmedicine.anatomical_structureMicroscopy FluorescenceRhodopsinCentrosomeCentrinbiology.proteinCalciumCattleElectrophoresis Polyacrylamide Gelsense organsTransducinProtein BindingThe Journal of biological chemistry
researchProduct