Search results for "Affinity Labels"

showing 10 items of 27 documents

8-Azido-adenosine 5'-triphosphate as a Photoaffinity Label for Bacterial F1 ATPase

1978

1. 8-Azido-adenosine 5'-triphosphate (n83ATP) is a suitable photoaffinity label for F1 ATPase from Micrococcus luteus. The nucleotide is a substrate in the presence of bivalent cations and inhibits the enzyme irreversibly upon irradiation with ultraviolet light above 300 nm. 2. More than 80% of the label is covalently bound to the beta subunits in the presence of bivalent cations. Labeling and inactivation is decreased by protection with ADP, ATP or adenyl-5'-yl imidodiphosphate. To a much smaller degree the alpha subunits also become labeled. 3. n83AMP does not specifically bind to the beta subunits upon irradiation. Like n83ATP and n83ADP, it also labels the alpha subunits to a small exte…

Macromolecular SubstancesUltraviolet RaysATPaseAffinity labelCooperativityBiochemistryMicrococcuschemistry.chemical_compoundAdenosine TriphosphateAdenine nucleotideUltraviolet lightMagnesiumNucleotideEdetic AcidAdenosine Triphosphataseschemistry.chemical_classificationPhotolysisbiologyAdenine NucleotidesChemistryAffinity LabelsBiochemistrybiology.proteinCalciumAdenosine triphosphateATP synthase alpha/beta subunitsEuropean Journal of Biochemistry
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Synthesis and characterization of biotinylated and photoactivatable neuroleptics. Novel bifunctional probes for dopamine receptors

1992

Abstract We have synthesized and characterized a series of novel derivatives of established antagonists of the neurotransmitter dopamine, i.e. butyrophenones, hexahydrocarbolines and phenothiazenes. All derivatives were biotinylated, some of them carried an additional (photoactivatable) azido group. In the case of butyrophenones, the structural modifications were introduced at the aliphatic keto group and/or the heterocyclic ring system, both modifications resulting in significant decreases in binding affinity to dopamine D 2 and dopamine D 1 receptor subtypes. Biotinylation of hexahydrocarbolines significantly increased their binding affinity to D 1 receptors, with the affinity for D 2 rec…

Magnetic Resonance SpectroscopySpectrophotometry InfraredPhotochemistryButyrophenoneStereochemistryBiotinIn Vitro TechniquesLigandsBinding CompetitiveReceptors DopamineStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDopaminemedicineAnimalsNeurotransmitterReceptor030304 developmental biologyPharmacology0303 health sciencesDopamine antagonistAffinity LabelsBenzazepineschemistryBiochemistrySpiperoneDopamine receptorBiotinylationCattleButyrophenones030217 neurology & neurosurgeryAntipsychotic Agentsmedicine.drugEuropean Journal of Pharmacology: Molecular Pharmacology
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Organotypic rat cerebellar slice culture as a model to analyze the molecular pharmacology of GABAA receptors

2002

The preservation of the neuronal circuitry in rat cerebellar slice cultures provides an advantage in monitoring the development and characterizing the pharmacology of GABA(A) receptor subtypes. Sprague-Dawley rats, 8-11 days of age, were decapitated, their cerebella were cut into 400-microm slices and transferred into culture dishes. Cell viability and organotypic cerebellar organization of the culture remained well preserved up to 3 weeks. Autoradiographic procedures were introduced in these advanced culture technique and employed [(3)H]Ro 15-4513 in the absence and presence of 10 microM diazepam to visualize all benzodiazepine (BZD) and diazepam-insensitive (DIS) binding sites, respective…

MaleAgonistAzidesCerebellumCell Survivalmedicine.drug_classProtein subunitBiologyPharmacologyRats Sprague-DawleyBenzodiazepinesCerebellumCulture TechniquesmedicineAnimalsPharmacology (medical)Viability assayReceptorCells CulturedBiological PsychiatryPharmacologyBenzodiazepineBinding SitesGABAA receptorAffinity LabelsReceptors GABA-ARatsPsychiatry and Mental healthmedicine.anatomical_structureAnimals NewbornNeurologyOrgan SpecificityNeurology (clinical)NeuroscienceDiazepammedicine.drugEuropean Neuropsychopharmacology
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Characterization of γ-aminobutyrate type A receptors with atypical coupling between agonist and convulsant binding sites in discrete brain regions

2001

Abstract γ-Aminobutyric acid type A (GABA A ) receptor ionophore ligand t -[ 35 S]butylbicyclophosphorothionate ([ 35 S]TBPS) was used in an autoradiographic assay on brain cryostat sections to visualize and characterize atypical GABA-insensitive [ 35 S]TBPS binding previously described in certain recombinant GABA A receptors and the cerebellar granule cell layer. Picrotoxinin-sensitive but 1-mM GABA-insensitive [ 35 S]TBPS binding was present in the rat cerebellar granule cell layer, many thalamic nuclei, subiculum and the internal rim of the cerebral cortex, amounting in these regions up to 6% of the basal binding determined in the absence of exogenous GABA. Similar binding properties wer…

MaleAgonistAzidesmedicine.medical_specialtyCerebellumSesterterpenesmedicine.drug_classLoreclezoleConvulsantsBiologySulfur RadioisotopesTritiumBinding CompetitiveBenzodiazepinesRadioligand AssayCellular and Molecular Neurosciencechemistry.chemical_compoundThalamusCerebellumInternal medicinemedicineAnimalsHumansPicrotoxinRats WistarBinding siteReceptorGABA AgonistsMolecular Biologygamma-Aminobutyric AcidMuscimolGABAA receptorAffinity LabelsBridged Bicyclo Compounds HeterocyclicReceptors GABA-AGranule cellRatsEndocrinologymedicine.anatomical_structurenervous systemMuscimolchemistryBiophysicsChickensmedicine.drugMolecular Brain Research
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Altered receptor subtypes in the forebrain of GABAA receptor δ subunit-deficient mice: recruitment of γ2 subunits

2002

A GABA(A) receptor delta subunit-deficient mouse line was created by homologous recombination in embryonic stem cells to investigate the role of the subunit in the brain GABA(A) receptors. High-affinity [(3)H]muscimol binding to GABA sites as studied by ligand autoradiography was reduced in various brain regions of delta(-/-) animals. [(3)H]Ro 15-4513 binding to benzodiazepine sites was increased in delta(-/-) animals, partly due to an increment of diazepam-insensitive receptors, indicating an augmented forebrain assembly of gamma 2 subunits with alpha 4 subunits. In the western blots of forebrain membranes of delta(-/-) animals, the level of gamma 2 subunit was increased and that of alpha …

MaleAzidesProtein subunitBiologyTritiumSynaptic TransmissionIon ChannelsGABAA-rho receptorInterleukin 10 receptor alpha subunitBenzodiazepinesMiceRadioligand Assaychemistry.chemical_compoundAnimalsReceptorGABA Agonistsgamma-Aminobutyric AcidMice KnockoutNeuronsBinding SitesMuscimolGABAA receptorGeneral NeuroscienceBrainAffinity LabelsNeural InhibitionReceptors GABA-AMolecular biologynervous systemMuscimolchemistryMutationForebrainFemaleCys-loop receptorsNeuroscience
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2,8-Diazido-ATP — a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1 in ATP synthase (from thermophilic b…

1995

Abstract To demonstrate the direct interfacial position of nucleotide binding sites between subunits of proteins we have synthesized the bifunctional photoaffinity label 2,8-diazidoadenosine 5′-triphosphate (2,8-DiN3ATP). UV irradiation of the F1-ATPase (TF1) from the thermophilic bacterium PS3 in the presence of 2,8-DiN3ATP results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of α-β crosslinks. The results confirm an interfacial localization of all the nucleotide binding sites on TF1.

Models MolecularAzidesNucleotide binding siteLightStereochemistryImmunoblottingBiophysicsDirect interfacial localizationShort lengthBiochemistry8-azidoadenosine 5'-triphosphatechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyGeneticsNucleotide binding sitesBifunctionalMolecular BiologyThermophilic bacterium PS3Photoaffinity cross-linkingchemistry.chemical_classificationATP synthasebiologyBacteriaThermophileAffinity LabelsCell BiologyProton-Translocating ATPasesEnzymeCross-Linking ReagentsBiochemistrychemistrybiology.proteinF1-ATPase: Short-length bifunctional photoaffinity labelFEBS Letters
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8-N(3)-3'-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue.

2001

A novel photoaffinity label, 8-N(3)-3'-biotinyl-ATP, has been synthesized. The introduction of an additional biotin residue is advantageous for easy detection of labeled proteins. This could be first tested by reaction with the F(1)-ATPase from the thermophilic bacterium PS3 (TF(1)). UV irradiation of TF(1) in the presence of 8-N(3)-3'-biotinyl-ATP results in a nucleotide-dependent binding of the analogue in the noncatalytic alpha and the catalytic beta subunits of TF(1), demonstrating the suitability of this analogue as a potential photoaffinity label. Reaction with the V(1)-ATPase, however, led to labeling of subunit E, which has been suggested as a structural and functional homologue of …

Models MolecularVacuolar Proton-Translocating ATPasesTime FactorsUltraviolet RaysProtein subunitATPaseBiophysicsCoated vesicleBiotinPhotoaffinity LabelsPhotoaffinity LabelsBiochemistryCatalysischemistry.chemical_compoundAdenosine TriphosphateBiotinBacterial ProteinsManducaAnimalsBinding siteMolecular BiologyBinding SitesPhotoaffinity labelingbiologyChemistryCell BiologyProton-Translocating ATPasesBiochemistryModels ChemicalSpectrophotometrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinCattleGamma subunitProtein BindingBiochemical and biophysical research communications
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Mapping of a binding site for ATP within the extracellular region of the Torpedo nicotinic acetylcholine receptor beta-subunit.

1997

Using 2,8,5'-[H-3]ATP as a direct photoaffinity label for membrane-bound nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata, we have identified a binding site for ATP in the extracellular region of the beta-subunit of the receptor. Photolabeling was completely inhibited in the presence of saturating concentrations of nonradioactive ATP, whereas neither the purinoreceptor antagonists suramin, theophyllin, and caffeine nor the nAChR antagonists alpha-bungarotoxin and d-tubocurarine affected the labeling reaction. Competitive and noncompetitive nicotinic agonists and Ca2+ increased the yield of the photoreaction by up to 50%, suggesting that the respective binding sites are allost…

Molecular Sequence DataPhotoaffinity LabelsReceptors NicotinicTorpedoTritiumBiochemistryPeptide Mappingchemistry.chemical_compoundGanglion type nicotinic receptorAdenosine TriphosphateAdenine nucleotideAnimalsChymotrypsinTrypsinAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisCell MembranePeptide FragmentsNicotinic acetylcholine receptorNicotinic agonistBiochemistrychemistrybiology.proteinAlpha-4 beta-2 nicotinic receptorExtracellular SpaceAdenosine triphosphateSequence AnalysisATP synthase alpha/beta subunitsBiochemistry
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Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

1994

UV irradiation of the ATPase (CF1) from spinach chloroplasts in the presence of 3'-arylazido-beta-alanyl-8-azido ATP (8,3'-DiN3ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF1.

Nucleotide binding siteAzidesChloroplastsStereochemistryPhotochemistryAffinity labelATPaseBiophysicsBiochemistryChloroplastF1ATPasechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyVegetablesGeneticsBinding siteChenopodiaceaeInterfacial localizationMolecular BiologyPhotoaffinity cross-linkingchemistry.chemical_classificationbiologyfood and beveragesAffinity LabelsCell Biologybiology.organism_classificationChloroplastProton-Translocating ATPasesEnzymeCross-Linking Reagentschemistrybiology.proteinSpinach chloroplastAdenosine triphosphateFEBS letters
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Identification of Purine Binding Sites on Torpedo Acetylcholine Receptor

1994

Electrophysiological studies from this and other laboratories have suggested a direct action of ATP on nicotinic acetylcholine receptors (nAChR). To determine the site of binding of this purine derivative, we have covalently modified the nAChR from Torpedo marmorata electrocytes employing 2-[3H]-8-azido-ATP as a photoactivable affinity label. Covalently attached radioactivity was predominantly found in the beta-polypeptide of the receptor. Based on the results of protection studies with several nAChR ligands whose target sites at the receptor are known, we conclude that the purine site(s) differ from those of acetylcholine and of physostigmine, galanthamine and related ligands, and those of…

PharmacologyPurineAzidesBinding SitesbiologyChemistryAffinity labelAffinity LabelsReceptors NicotinicTorpedolaw.inventionchemistry.chemical_compoundAdenosine TriphosphateNicotinic agonistBiochemistrylawbiology.proteinmedicineAnimalsBinding siteReceptorTorpedoAcetylcholinemedicine.drugAcetylcholine receptorJournal of Receptor Research
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