Search results for "binding sites"

showing 10 items of 636 documents

In vivo biodistribution and lifetime analysis of cy5.5-conjugated rituximab in mice bearing lymphoid tumor xenograft using time-domain near-infrared …

2008

Rituximab is a chimeric monoclonal antibody directed against human CD20 antigen, which is expressed on B-cell lymphocytes and on the majority of B-cell lymphoid malignancies. Herein we report the conjugate of rituximab with the near-infrared (NIR) fluorophore Cy5.5 (RI-Cy5.5) as a tool for in vitro, in vivo, and ex vivo NIR time-domain (TD) optical imaging. In vitro, RI-Cy5.5 retained biologic activity and led to elevated cell-associated fluorescence on tumor cells. In vivo, TD optical imaging analysis of RI-Cy5.5 injected into lymphoma-bearing mice revealed a slow tumor uptake and a specific long-lasting persistence of the probe within the tumor. Biodistribution studies after intraperiton…

BiodistributionPathologymedicine.medical_specialtylcsh:Medical technologyLymphomamedicine.medical_treatmentIntraperitoneal injectionTransplantation HeterologousBiomedical EngineeringCarbocyanineMice SCIDBiologyIntestinal absorptionAntibodies Monoclonal Murine-DerivedMiceIn vivomedicineAnimalsHumansRadiology Nuclear Medicine and imagingAnimals; Antibodies Monoclonal; Antibodies Monoclonal Murine-Derived; Binding Sites; Carbocyanines; Cell Division; Female; Humans; Immunohistochemistry; Intestinal Absorption; Lymph Nodes; Lymphoma; Mice; Mice SCID; Neoplasm Transplantation; Rituximab; Transplantation Heterologouslcsh:QH301-705.5Binding SitesAnimaltechnology industry and agricultureBinding SiteAntibodies MonoclonalLymph NodeCarbocyaninesCondensed Matter PhysicsImmunohistochemistryTransplantationlcsh:Biology (General)lcsh:R855-855.5Intestinal AbsorptionMonoclonalMolecular MedicineImmunohistochemistryFemaleLymph NodesRituximabEx vivoCell DivisionNeoplasm TransplantationBiotechnologyHuman
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New evidence for the multiplicity of ubiquinone- and inhibitor-binding sites in the mitochondrial complex I.

2000

Determination of the number of ubiquinone- and inhibitor-binding sites in the mitochondrial complex I (NADH:ubiquinone oxidoreductase) is a controversial question with a direct implication for elaborating a suitable model to explain the bioenergetic mechanism of this complicated enzyme. We have used combinations of both selective inhibitors and common ubiquinone-like substrates to demonstrate the multiplicity of the reaction centers in the complex I in contrast with competition studies that have suggested the existence of a unique binding site for ubiquinone. Our results provide new evidence for the existence of at least two freely exchangeable ubiquinone-binding sites with different specif…

BioenergeticsStereochemistryUbiquinoneSubmitochondrial ParticlesBiophysicsBiologyIn Vitro TechniquesBiochemistryModels BiologicalMitochondria HeartSubstrate SpecificityOxidoreductaseAnimalsNADH NADPH OxidoreductasesBinding siteMultiplicity (chemistry)Molecular Biologychemistry.chemical_classificationNADH-Ubiquinone OxidoreductaseBinding SitesElectron Transport Complex IKineticsEnzymechemistryBiochemistryCattleEnergy MetabolismMitochondrial Complex IArchives of biochemistry and biophysics
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Electrochemical probe for the monitoring of DNA-protein interactions.

2010

Self-assembly of thiol-terminated oligonucleotides on gold substrates provides a convenient way for DNA-functionalized surfaces. Here we describe the development of an electrochemical assay for the detection of DNA-protein interactions based on the modification of the electrochemical response of methylene blue (MB) intercalated in the DNA strands. Using a functionalized electrode with double stranded DNA carrying T3 RNA polymerase binding sequence, we show a substantial attenuation of the current upon the DNA-protein interaction. Moreover, a Langmuir binding isotherm for T3 RNA polymerase (T3 Pol) gives a dissociation constant K(D) equal to 0.46+/-0.23 microM. Such value is 100 times lower …

Biomedical EngineeringBiophysicsBiosensing TechniquesIn Vitro Techniqueschemistry.chemical_compoundViral ProteinsElectrochemistrymedicineT7 RNA polymeraseAnimalsBovine serum albuminBinding sitePromoter Regions Geneticchemistry.chemical_classificationBinding SitesbiologyBase SequenceOligonucleotideProteinsSerum Albumin BovineGeneral MedicineDNADNA-Directed RNA PolymerasesElectrochemical TechniquesMolecular biologyDissociation constantMethylene BlueEnzymechemistryDNA Viralbiology.proteinBiophysicsCattleGoldMethylene blueDNABiotechnologymedicine.drugBiosensorsbioelectronics
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Valproate and Short-Chain Fatty Acids Activate Transcription of the Human Vitamin D Receptor Gene through a Proximal GC-Rich DNA Region Containing Tw…

2022

The vitamin D receptor (VDR) mediates 1,25-dihydroxyvitamin D3 pleiotropic biological actions through transcription regulation of target genes. The expression levels of this ligand-activated nuclear receptor are regulated by multiple mechanisms both at transcriptional and post-transcriptional levels. Vitamin D3 is the natural VDR activator, but other molecules and signaling pathways have also been reported to regulate VDR expression and activity. In this study, we identify valproic acid (VPA) and natural short-chain fatty acids (SCFAs) as novel transcriptional activators of the human VDR (hVDR) gene. We further report a comprehensive characterization of VPA/SCFA-responsive elements in the 5…

BioquímicaBiologiaVDR induction; human VDR promoter; valproic acid; SCFA; Sp1.Binding SitesNutrition and DieteticsSp1 Transcription FactorValproic AcidDNAHumansReceptors Calcitriollipids (amino acids peptides and proteins)ChildPromoter Regions GeneticFood Science
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Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
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Mutation of the important Tyr-33 residue of chicken avidin: functional and structural consequences

2002

The strong interaction between avidin and biotin is so tight (dissociation constant 10-15M) that conditions usually sufficient for protein denaturing fail to dislodge biotin from the avidin—biotin complex. This kind of irreversible binding hinders the use of avidin in applications such as affinity purification or protein immobilization. To address this concern, we have constructed a series of mutants of the strategically positioned Tyr-33 in order to study the role of this residue in biotin binding, and to create avidin variants with more reversible ligand-binding properties. Unexpectedly, an avidin mutant in which Tyr-33 was replaced with phenylalanine (Avm-Y33F) displayed similar biotin-b…

Biotin bindingBiotinPlasma protein bindingLigandsBiochemistrychemistry.chemical_compoundBiotinAnimalsBinding siteMolecular BiologyBinding SitesMolecular StructurebiologyChemistryTemperatureHydrogen BondingCell BiologyHydrogen-Ion ConcentrationAvidinOxygenDissociation constantBiochemistryBiotinylationMutationMutagenesis Site-Directedbiology.proteinTyrosineProtein quaternary structureEndopeptidase KChickensProtein BindingResearch ArticleAvidinBiochemical Journal
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Demonstration of High-Affinity Binding Sites for C3a Anaphylatoxin on Guinea-Pig Platelets

1978

3H-serotonin release from guinea-pig platelets was demonstrated to be the consequence of C3a binding to these cells. A Scatchard analysis of dose-response data of the 125I-C3a binding pattern to guinea-pig platelets pointed to the existence of binding sites with high and low affinity for the C3a molecule (HA and LA receptors). HA receptors are specific for C3a with intact C-terminal arginine. whereas C3adesarg only interacts with LA receptors. The release of serotonin may be induced by a combined reaction of C3a with HA receptors and LA receptors on the platelet membrane.

Blood PlateletsAnaphylatoxinsSerotoninBinding SitesArginineChemistryGuinea PigsImmunologyTemperaturechemical and pharmacologic phenomenaCarboxypeptidasesComplement C3General MedicineGuinea pigBiochemistryAnimalsProtease-activated receptorPlateletAnaphylatoxinSerotoninBinding sitePeptidesReceptorScandinavian Journal of Immunology
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Resolving Binding Events on the Multifunctional Human Serum Albumin

2020

Abstract Physiological processes rely on initial recognition events between cellular components and other molecules or modalities. Biomolecules can have multiple sites or mode of interaction with other molecular entities, so that a resolution of the individual binding events in terms of spatial localization as well as association and dissociation kinetics is required for a meaningful description. Here we describe a trichromatic fluorescent binding‐ and displacement assay for simultaneous monitoring of three individual binding sites in the important transporter and binding protein human serum albumin. Independent investigations of binding events by X‐ray crystallography and time‐resolved dyn…

Boron Compounds540 Chemistry and allied sciencesalbumin bindingIbuprofenSerum Albumin HumanMolecular Dynamics SimulationCrystallography X-Ray01 natural sciencesBiochemistryFluorescenceDrug DiscoverymedicineHumansSpatial localizationmulticolor assayskinetics investigationsGeneral Pharmacology Toxicology and PharmaceuticsBinding sitePharmacologychemistry.chemical_classificationBinding SitesMolecular Structure010405 organic chemistryBinding proteinBiomoleculeCommunicationOrganic ChemistryLauric AcidsTransporterdrug interactionsHuman serum albuminFluorescenceCommunications0104 chemical sciences010404 medicinal & biomolecular chemistry4-Chloro-7-nitrobenzofurazanchemistry540 ChemieBiophysicsMolecular MedicineDissociation kineticsswitchSENSE technologyWarfarinmedicine.drugChemmedchem
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Shared Binding Sites for the Bacillus thuringiensis Proteins Cry3Bb, Cry3Ca, and Cry7Aa in the African Sweet Potato Pest Cylas puncticollis (Brentida…

2014

ABSTRACT Bacillus thuringiensis Cry3Bb, Cry3Ca, and Cry7Aa have been reported to be toxic against larvae of the genus Cylas , which are important pests of sweet potato worldwide and particularly in sub-Saharan Africa. However, relatively little is known about the processing and binding interactions of these coleopteran-specific Cry proteins. The aim of the present study was to determine whether Cry3Bb, Cry3Ca, and Cry7Aa proteins have shared binding sites in Cylas puncticollis to orient the pest resistance strategy by genetic transformation. Interestingly, processing of the 129-kDa Cry7Aa protoxin using commercial trypsin or chymotrypsin rendered two fragments of about 70 kDa and 65 kDa. N-…

Brush borderBacillus thuringiensisBiological pest controlHemolysin ProteinsApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEnvironmental MicrobiologymedicineAnimalsIpomoea batatasBinding sitePlant DiseasesBinding SitesChymotrypsinBacillus thuringiensis ToxinsEcologybiologyfungiTrypsinbiology.organism_classificationColeopteraEndotoxinsLarvabiology.proteinPEST analysisFood ScienceBiotechnologymedicine.drugApplied and Environmental Microbiology
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Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

2003

Abstract Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1…

Brush borderBacterial ToxinsBacillus thuringiensisGenetically modified cropsBinding CompetitiveBiochemistryMicrobiologyIodine RadioisotopesRadioligand AssayBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyBinding SitesMicrovillibiologyHeliothis virescensCytoplasmic Vesiclesfungifood and beveragesPlutellabiology.organism_classificationRecombinant ProteinsLepidopteraKineticsBt cottonCry1AcLarvaInsect ScienceProtein BindingPink bollwormInsect Biochemistry and Molecular Biology
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