Search results for "Affinity label"

showing 10 items of 39 documents

Direct identification of the agonist binding site in the human brain cholecystokinin-B receptor

1999

In investigating the agonist binding site of the human brain cholecystokininB receptor (CCKBR), we employed the direct protein chemical approach using a photoreactive tritiated analogue of sulfated cholecystokinin octapeptide, which contains the p-benzoylbenzoyl moiety at the N-terminus, followed by purification of the affinity-labeled receptor to homogeneity. This probe bound specifically, saturably, and with high affinity (KD = 1.2 nM) to the CCKBR and has full agonistic activity. As the starting material for receptor purification, we used stably transfected HEK 293 cells overexpressing functional CCKBR. Covalent labeling of the WGA-lectin-enriched receptor revealed a 70-80 kDa glycoprote…

ElectrophoresisModels MolecularAgonistProtein Conformationmedicine.drug_classPeptidePhotoaffinity LabelsTritiumBiochemistryMass SpectrometrySincalidemedicineHumansBinding siteReceptorCells Culturedchemistry.chemical_classificationBinding SitesEdman degradationHEK 293 cellsBrainMolecular biologyReceptor Cholecystokinin BchemistryBiochemistryCholecystokinin B receptorChromatography GelMutagenesis Site-DirectedReceptors CholecystokininCholecystokininGlycoproteinSequence Analysis
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A constitutively active pituitary adenylate cyclase activating polypeptide (PACAP) type I receptor shows enhanced photoaffinity labeling of its highl…

2001

Abstract In the present study, we have analyzed a previously identified constitutively active pituitary adenylate cyclase activating polypeptide (PACAP) type I (PAC1) receptor with a deletion of the single amino acid residue Glu 261 (Y.-J. Cao, G. Gimpl, F. Fahrenholz, A mutation of second intracellular loop of pituitary adenylate cyclase activating polypeptide type I receptor confers constitutive receptor activation, FEBS Lett. 469 (2000)). This glutamic acid residue is highly conserved within the second intracellular loop of class II G protein-coupled receptors and may thus be of importance for many members of this receptor class. To explore the molecular characteristics of this mutant re…

GlycosylationBiophysicsReceptors Pituitary Adenylate Cyclase-Activating PolypeptideBiochemistryCyclaseAmidohydrolasesStructural BiologyEnzyme-linked receptorAnimalsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase5-HT5A receptorReceptors Pituitary HormoneReceptorMolecular BiologyCOS cellsPhotoaffinity labelingChemistryAffinity LabelsGlutamic acidMolecular biologyRatsMolecular WeightBiochemistryCOS CellsMutationSignal transductionAdenylyl CyclasesPlasmidsReceptors Pituitary Adenylate Cyclase-Activating Polypeptide Type IBiochimica et biophysica acta
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Photoaffinity Labeling and Photoaffinity Cross-Linking of Phosphofructokinase-1 from Saccharomyces cerevisiae by 8-Azidoadeninenucleotides

2001

Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of four alpha- and four beta-subunits, each of them carrying catalytic and regulatory bindings sites for MgATP. In this paper, various photoaffinity labels, such as 8-azidoadenosine 5'-triphosphate, 8-azido-1,N6-ethenoadenosine 5'-triphosphate, and 8-N3-3'(2')-O-biotinyl-8-azidoadenosine 5'-triphosphate have been used to study their interaction with the enzyme in the dark and during irradiation. All nucleotidetriphosphates function as phosphate donor forming fructose 1,6-bisphosphate from fructose 6-phosphate. However, the kinetic analysis revealed distinctly differences between them. Photolabeling causes a decrease in enzyme a…

LightPhosphofructokinase-1Blotting WesternSaccharomyces cerevisiaeBiophysicsPhotoaffinity LabelsSaccharomyces cerevisiaePhotoaffinity LabelsBiochemistryAdenosine TriphosphateFructosediphosphatesChymotrypsinMagnesiumPhosphofructokinase 1Molecular Biologychemistry.chemical_classificationGel electrophoresisBinding SitesAffinity labelingbiologyPhotoaffinity labelingFructosephosphatesDarknessbiology.organism_classificationEnzyme assayKineticsProtein SubunitsCross-Linking ReagentsEnzymechemistryBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelArchives of Biochemistry and Biophysics
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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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In vitro modeling of the ternary interaction in juvenile hormone metabolism

1996

The gradual decline in juvenile hormone (JH) titer followed by its complete clearance early in the last larval instar is required for the onset of the metamorphosis of lepidopterous larvae. JH titer is regulated by both biosynthesis and degradation. Two major pathways for JH metabolism, ester hydrolysis and epoxide hydration, are due to JH esterase (JHE) and JH epoxide hydrolase (JHEH), respectively. In vitro experiments designed to elucidate the molecular mechanism of JH metabolism are described. First, microsomal JHEH in Manduca sexta eggs was identified by using photoaffinity analogs of JH, and purified to homogeneity with ion exchange and hydroxylapatite columns. Purified JHEH from M. s…

Manduca sextaJH binding proteinJH epoxide hydrolaseJH esterasephotoaffinity labelingArchives of Insect Biochemistry and Physiology
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Purification and reassessment of ligand binding by the recombinant, putative juvenile hormone receptor of the tobacco hornworm, Manduca sexta

1996

The 29 kDa protein from the larval epidermis of the tobacco hornworm, Manduca sexta, that specifically bound photoaffinity analogs of JH I and JH II was produced by a recombinant baculovirus (rJP29). The higher of the two molecular weight forms made corresponded to a protein that could be formed by read‐through of the TGA termination codon to the following TAA. The previously reported, apparent high affinity binding of [methyl‐3H]‐JH I by rJP29 as measured by the dextran‐coated charcoal (DCC) assay [Palli et al., Proc Natl Acad Sci USA 91:6191–6195 (1994)] was found to be artifactual due to endogenous cellular esterases that co‐purified with rJP29 through both DEAE cellulose and MonoQ chrom…

Manduca sextaTn5 cellsjuvenile hormone receptorcellular esterasesSf21 cellsrecombinant baculovirus proteinJH esterasephotoaffinity labelingArchives of Insect Biochemistry and Physiology
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