Search results for "label"

showing 10 items of 797 documents

High-performance and ion-exchange chromatography and chromatofocusing of the human uterine progesterone receptor: its application to the identificati…

1984

Two independent lines of evidence were used to identify the human uterine progesterone receptor. First, three differently tritiated progestogens (Org 2058, R 5020, progesterone) were used for reversible labelling of the receptor. Secondly, the highly potent affinity label 21-[3H]dehydro Org 2058 was used to label covalently the steroid-specific binding site of the receptor. The labelled cytosols were chromatographed on a Mono Q high-performance anion-exchange column in the absence or presence of a high molar excess of the respective unlabelled competitor steroids. In the case of 21-[3H]dehydro Org 2058, Org 2058 was used as the unlabelled competitor. After elution with a NaCl gradient, the …

Chemical Phenomenamedicine.medical_treatmentAffinity labelIon chromatographyIn Vitro TechniquesBinding CompetitiveBiochemistryChromatography AffinityAnalytical ChemistrySteroidCytosolPregnenedionesProgesterone receptormedicineHumansPolyacrylamide gel electrophoresisChromatography High Pressure LiquidChromatographybiologyChemistryChromatofocusingIsoelectric focusingElutionUterusOrganic ChemistryGeneral MedicineChromatography Ion ExchangeChemistrybiology.proteinElectrophoresis Polyacrylamide GelFemaleIsoelectric FocusingReceptors ProgesteroneJournal of Chromatography A
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Acute Toxicity Testing in Vitro and the Classification and Labelling of Chemicals

1996

Chemical compoundbusiness.industryGeneral MedicinePharmacologyToxicologyGeneral Biochemistry Genetics and Molecular BiologyToxicologyMedical Laboratory Technologychemistry.chemical_compoundInvestigation methodschemistryLabellingToxicityMedicineToxicokineticsbusinessAcute toxicity testingAlternatives to Laboratory Animals
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Studies in organic mass spectrometry. Part 24† Electron ionization mass spectra of some aryl(2-nitrobenzo[b]thiophen-3-yl)amines

1999

The main fragmentation routes of eighteen title compounds and of three 5-chloro derivatives have been investigated with the aid of linked scan (B/E = constant) spectrometry, accurate mass measurements and deuterium labelling. Copyright © 1999 John Wiley & Sons, Ltd.

ChemistryArylOrganic ChemistryAnalytical chemistryMass spectrometryMedicinal chemistryAnalytical Chemistrychemistry.chemical_compoundFragmentation (mass spectrometry)DeuteriumLabellingMass spectrumSpectroscopyElectron ionizationRapid Communications in Mass Spectrometry
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Structure and stability of hexadentate complexes of ligands based on AAZTA for efficient PET labelling with gallium-68

2012

Pre-organised tricarboxylate ligands based on 6-amino-perhydro-1,4-diazepine bind (68)Ga rapidly and selectively in acetate buffer at pH 4 to 7, forming kinetically stable complexes suitable for use in PET imaging.

ChemistryMetals and Alloyschemistry.chemical_elementGeneral ChemistryPet imagingTricarboxylateCombinatorial chemistryCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsLabellingMaterials ChemistryCeramics and CompositesOrganic chemistryGalliumChem. Commun.
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Site-Specific Information on Membrane Protein Folding by Electron Spin Echo Envelope Modulation Spectroscopy

2010

Compared to folding of soluble proteins, folding of membrane proteins is complicated by the fact that it requires an amphiphilic environment. Few existing techniques can provide structurally resolved information on folding kinetics. For the major plant light harvesting complex LHCII, it is demonstrated that changes in water accessibility of a particular amino acid residue can be followed during folding by measuring the hyperfine interaction of spin labels with deuterium nuclei of heavy water. The incorporation of residue 196 into the hydrophobic core of a detergent micelle was investigated. The technique provides a time constant that is similar to the one found with fluorescence spectroscop…

ChemistryPhi value analysisSite-directed spin labelinglaw.inventionFolding (chemistry)CrystallographylawLattice proteinBiophysicsGeneral Materials ScienceProtein foldingDownhill foldingPhysical and Theoretical ChemistryElectron paramagnetic resonanceSpin labelThe Journal of Physical Chemistry Letters
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Profiling of RNA modifications by multiplexed stable isotope labelling

2014

The combination of (15)N/(13)C stable isotope labelling (SIL) and LC-MS/MS revealed a total of 52 modifications in RNA from E. coli and yeast, including 10 previously undescribed modifications. Two modifications, N-ribosylnicotinamide and 2-methylthioadenosine, were newly detected in species hitherto thought not to contain these modifications.

ChemistryStable isotope ratioMetals and AlloysRNASaccharomyces cerevisiaeGeneral ChemistryTandem mass spectrometryCatalysisYeastSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsBiochemistryTandem Mass SpectrometryIsotope LabelingLabellingEscherichia coliMaterials ChemistryCeramics and CompositesRNAChromatography LiquidChemical Communications
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Two-step radiosynthesis of [18F]FE-β-CIT and [18F]PR04.MZ

2013

The cocaine-derived dopamine reuptake inhibitors FE-β-CIT (8-(2-fluoroethyl)-3-(4-iodophenyl)-8-azabicyclo[3.2.1]octane-2-carboxylic acid methyl ester) (1) and PR04.MZ(8-(4-fluorobut-2-ynyl)-3-p-tolyl-8-azabicyclo[3.2.1]octane-2-carboxylic acid methyl ester) (2) were labelled with (18)F-fluorine using a two-step route. 2-[(18)F]Fluoroethyltosylate and 4-[(18)F]fluorobut-2-yne-1-yl tosylate were used as labelling reagents, respectively. Radiochemically pure (>98%) [(18)F]FE-β-CIT and [(18)F]PRD04.MZ (32-86 GBq/µmol) were obtained after a synthesis time of 100 min in about 25% non-decay-corrected overall yield.

ChemistryStereochemistryOrganic ChemistryRadiosynthesisTwo stepBiochemistryMedicinal chemistryAnalytical ChemistryLabellingYield (chemistry)ReagentDrug DiscoveryRadiology Nuclear Medicine and imagingSpectroscopyJournal of Labelled Compounds and Radiopharmaceuticals
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Photobinding of Tiaprofenic Acid and Subprofen to Proteins and Cells: A Combined Study Using Radiolabeling, Antibodies and Laser Flash Photolysis of …

1998

Drug photoallergy is a matter of current concern. It involves the formation of drug-protein photoadducts (photoantigens) that may ultimately trigger an immunological response. Tyrosine residues appear to be key binding sites in proteins. The present work has investigated the photobinding of tiaprofenic and (TPA) and the closely related isomer suprofen (SUP) to proteins and cells by means of radioactive labeling and drug-directed antibodies. To ascertain whether preassociation with the protein may play a role in photoreactivity, two model bichromophoric compounds (TPA-Tyr and SUP-Tyr) have been prepared and studied by laser flash photolysis. The results of this work show that (a) TPA and SUP…

ChemistryStereochemistrySuprofenGeneral MedicinePlasma protein bindingPhotochemistryBiochemistryCell membranemedicine.anatomical_structureLabellingmedicineFlash photolysisPhysical and Theoretical ChemistryBinding siteTyrosineTiaprofenic acidmedicine.drug
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Filling the “green gap” of the major light-harvesting chlorophyll a/b complex by covalent attachment of Rhodamine Red

2009

AbstractThe major light-harvesting chlorophyll a/b complex (LHCII) greatly enhances the efficiency of photosynthesis in green plants. Recombinant LHCII can be assembled in vitro from its denatured, bacterially expressed apoprotein and plant pigments. This makes it an interesting candidate for biomimetic light-harvesting in photovoltaic applications. Due to its almost 20 pigments bound per apoprotein, LHCII absorbs efficiently in the blue and red spectral domains of visible light but less efficiently in the green domain, the so-called “green gap” in its absorption spectrum. Here we present a hybrid complex of recombinant LHCII with organic dyes that add to LHCII absorption in the green spect…

ChlorophyllLHCIIProtein FoldingFRET (Förster resonance energy transfer)Chlorophyll aAbsorption spectroscopyBiophysicsPhotosynthesisPhotochemistryBiochemistryRhodamineLight-harvesting complexchemistry.chemical_compoundPhotosynthesisFluorescent DyesRhodaminesChlorophyll Afood and beveragesSite-specific labelingCell BiologyMaleimide dyeB vitaminsSolar spectrumchemistryChlorophyllVisible spectrumBiochimica et Biophysica Acta (BBA) - Bioenergetics
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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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