Search results for " gel"

showing 10 items of 1051 documents

Identification of a cell surface-associated protein involved in mouse neural cell aggregation by means of antibodies against the sponge aggregation f…

1989

Polyclonal antibodies were raised against the purified aggregation factor (AF) from the sponge Geodia cydonium to elucidate possible immunological relationships between adhesion molecules of lower multicellular eukaryotic systems (sponges) and those of vertebrates. This anti-AF recognized a series of polypeptides associated with the AF, among them also a polypeptide with a Mr of 47,000 (p47). The formation of the antibody-p47 immunocomplexes could be prevented by adsorbing the anti-AF with a brain extract from DBA/2J mice. Moreover, this brain polypeptide inhibited the AF-mediated aggregation of sponge cells. Interestingly, the anti-AF recognized a p37 molecule in the brains of 2- to 3-day-…

CellBlotting WesternSpleenNerve Tissue ProteinsBiochemistryAntibodiesImmunoglobulin Fab FragmentsMicemedicineAnimalsPolyacrylamide gel electrophoresisCell AggregationNeuronsbiologyCell adhesion moleculeCell MembraneBrainProteinsMolecular biologyImmunohistochemistryCell aggregationBlotmedicine.anatomical_structurePolyclonal antibodiesbiology.proteinElectrophoresis Polyacrylamide GelAntibodyPeptidesCell Adhesion MoleculesMembrane biochemistry
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Mapping of phenytoin-inducible cytochrome P450 immunoreactivity in the mouse central nervous system

1991

Abstract The distribution of phenytoin-inducible cytochrome P450 in non-treated mouse brain and spinal cord was analysed immunohistochemically using polyclonal antibodies against phenytoin-induced mouse cerebral microsomal P450. This P450 protein was proved in Ouchterlony [Volk B. et al. (1988) Neurosci. Lett. 84 , 219–224], Western blot, and immunohistochemical analyses to be reactive to the specific antibodies and an IgG fraction raised against phenobarbital-induced rat liver microsomal P450IIB1. The phenytoin-induced P450 is designated P450IIB1 * because immunologically it is comparable with P450IIB1; however, it has not yet been analysed for other characteristics of this enzyme. Immunoc…

Central Nervous SystemMaleCerebellumPathologymedicine.medical_specialtyCentral nervous systemPyramidal TractsBiologyMiceCerebellummedicineNeuropilAnimalsNeuronsGeneral NeurosciencePontine nucleiSpinal cordImmunohistochemistryPonsMice Inbred C57BLmedicine.anatomical_structurenervous systemEnzyme InductionPhenytoinSteroid 11-beta-HydroxylaseElectrophoresis Polyacrylamide GelBrainstemEpendymaNeuroscience
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Identification of an Antigen Related to the Sea Urchin RNA-Binding Protein LP54 in Mammalian Central Nervous System

2001

LP54 is an RNA-binding protein involved in localization of maternal messengers in sea urchin egg and embryos. Using a polyclonal antibody directed against Paracentrotus lividus LP54 we detected a 66-kDa cross-reacting antigen in undifferentiated and differentiated SH-SY5Y human neuroblastoma cells. After treatment of undifferentiated cells with detergent, the 66-kDa antigen was found to be enriched in the cytoskeletal fraction. By Western blot the expression of this antigen was also analyzed in regions of the CNS and in tissues of the adult rat and its exclusive presence in the hippocampus and thalamus was revealed. The immunoreactivity with P. lividus antibody against LP54 in hippocampal l…

Central Nervous SystemRNA localizationOctoxynolBlotting WesternDetergentsRNA-binding proteinBinding CompetitiveHippocampusParacentrotus lividusThalamusWestern blotAntigenbiology.animalTumor Cells CulturedmedicineAnimalsHumansRNA MessengerMolecular BiologySea urchinCytoskeletonbiologymedicine.diagnostic_testRNA-Binding ProteinsCell Differentiationbiology.organism_classificationMolecular biologyRatsMicroscopy FluorescencePolyclonal antibodiesSea Urchinsbiology.proteinElectrophoresis Polyacrylamide GelAntibodyMicrotubule-Associated ProteinsMolecular Cell Biology Research Communications
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Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target memb…

1999

Vibrio cholerae cytolysin permeabilizes animal cell membranes. Upon binding to the target lipid bilayer, the protein assembles into homo-oligomeric pores of an as yet unknown stoichiometry. Pore formation has been observed with model liposomes consisting of phosphatidylcholine and cholesterol, but the latter were much less susceptible to the cytolysin than were erythrocytes or intestinal epithelial cells. We here show that liposome permeabilization is strongly promoted if cholesterol is combined with sphingolipids, whereby the most pronounced effects are observed with monohexosylceramides and free ceramide. These two lipid species are prevalent in mammalian intestinal brush border membranes…

CeramideCell Membrane PermeabilityPentamerProtein ConformationGalactosylceramidesBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundPhosphatidylcholinemedicineHumansLipid bilayerMolecular BiologyVibrio choleraeCells CulturedLiposomeSphingolipidsCytotoxinsBrainCell BiologyFluoresceinsLipid MetabolismMembraneCholesterolBiochemistrychemistryVibrio choleraeLiposomesElectrophoresis Polyacrylamide GelCytolysinIsoelectric FocusingThe Journal of biological chemistry
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Extraction of uranyl ions from aqueous solutions using silica-gel-bound macrocycles for alpha contaminated waste water treatment

2004

Abstract The efficiency for the extraction of U(VI) of new modified silica gels, namely N-tripropionate (or N-triacetate)-substituted tetraazamacrocycles-bound silica gels, has been studied. The effect of the nature of the ligand, the pH and the temperature was studied both in batch experiments as well as in continuous extraction. These silica gels are good candidates for the extraction of U(VI) when compared to a commercially available acid-type chelating resin. The breakthrough and regeneration tests showed that the total removal of U(VI) from a contaminated solution can be achieved by using a column packed with such tetraazamacrocycles-bound silica gels. Finally, the use of a modified si…

Chelating resinAqueous solutionSilica gelExtraction (chemistry)chemistry.chemical_elementAmericiumUraniumUranylBiochemistryAnalytical Chemistrychemistry.chemical_compoundchemistryEnvironmental ChemistrySolid phase extractionSpectroscopyNuclear chemistryAnalytica Chimica Acta
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Albumin binding and hydrophobic character of promazine and chlorpromazine metabolites.

1972

1. The binding of didesmethylpromazine, promazine N-oxide, 2-hydroxypromazine, promazine sulfoxide, monodesmethylpromazine sulfoxide, didesmethylchlorpromazine, chlorpromazine N-oxide, and chlorpromazine sulfoxide to bovine serum albumin was determined by means of sephadex gel filtration. 2. The albumin binding of these substances was characterized by the following parameters: the percentage α of free substance, the percentage β of bound substance, the binding constants K1, k+ and m, the number of binding sites per albumin molecule, and the free binding energy ΔFo. 3. The partition coefficients between n-octanol and buffer solution, pH 7.40, were measured for the above mentioned metabolites…

Chemical PhenomenaChlorpromazineStatistics as TopicPlasma protein bindingchemistry.chemical_compoundmedicineAnimalsBovine serum albuminChlorpromazinePromazinePromazinePharmacologyChromatographyBinding SitesbiologyAlbuminSulfoxideSerum Albumin BovineGeneral MedicineBuffer solutionChemistrychemistrySolubilitySephadexSulfoxidesbiology.proteinChromatography GelCattleNitrogen OxidesChlorinemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Isolation of oligopeptides from the water-soluble extract of goat cheese and their identification by mass spectrometry

2001

A procedure for the separation and identification of small peptides from the water-soluble fraction of a goat cheese was developed. The water-soluble extract was ultrafiltered (1000 Da membrane cutoff), and peptides were isolated by sequential chromatography: size exclusion chromatography (HPLC-grade water), anion exchange chromatography (phosphate buffer gradient), and semipreparative reverse-phase high-performance liquid chromatography (water/acetonitrile gradient). The fractions obtained were analyzed by combined mass spectrometry methods including electrospray ionization, liquid secondary ionization, and tandem mass spectrometry to identify and to confirm the sequences of 28 tri- to oct…

Chemical PhenomenaElectrospray ionizationSize-exclusion chromatographyMass spectrometryTandem mass spectrometry01 natural sciencesHigh-performance liquid chromatographyMass Spectrometry0404 agricultural biotechnologyCheeseCasein[SDV.IDA]Life Sciences [q-bio]/Food engineeringAnimalsAmino Acid SequenceChymosinChromatography High Pressure LiquidComputingMilieux_MISCELLANEOUSChromatographyChemistry PhysicalElutionChemistryGoats010401 analytical chemistryWater04 agricultural and veterinary sciencesGeneral Chemistry[SDV.IDA] Life Sciences [q-bio]/Food engineeringChromatography Ion Exchange040401 food science0104 chemical sciencesSolubilityChromatography GelGeneral Agricultural and Biological SciencesOligopeptides
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Biochemical analysis of class II antigens. Identification of a two- and a three-polypeptide chain complex of I-A locus equivalent molecules in the ra…

1983

The polypeptide chain composition of class II antigens from LEW rat spleen cells was studied utilizing cross-reactive mouse alloantiserum A. TH anti-A.TL (specificity anti-Iak) and the monoclonal antibodies MRC-OX6 and MRC-OX3 for immunoprecipitation. Two-dimensional gel mapping of A. TH anti-A. TL immunoprecipitates revealed that, as in the mouse, two groups of class II antigens exist corresponding to I-A and I-E locus equivalent structures. In the absence of reducing agents three monomeric chains α, 36 kDa (p36); γ, 33 kDa (p33); and β, 23 kDa (p23), were detected for I-A equivalent antigens, whereas I-E equivalent molecules separated into five monomeric chains: α, 37 kDa (p37); γ, 33 kDa…

Chemical PhenomenaReducing agentImmunoprecipitationmedicine.drug_classMice Inbred ADimerImmunologyGenes MHC Class IILocus (genetics)BiologyCross ReactionsMonoclonal antibodychemistry.chemical_compoundMiceAntigenmedicineImmunology and AllergyMoleculeAnimalsChemical PrecipitationAntilymphocyte SerumHistocompatibility Antigens Class IIAntibodies MonoclonalChromosome MappingRats Inbred StrainsRatsChemistryMonomerchemistryBiochemistryRats Inbred LewElectrophoresis Polyacrylamide GelPeptidesEuropean journal of immunology
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Preferential solvation of poly(methyl methacrylate) and a bisphenol A diglycidyl ether by size-exclusion chromatography

2004

The preferential adsorption coefficient, lambda, of poly(methyl methacrylate), PMMA, in solutions formed by an epoxy resin in tetrahydrofuran (THF), was studied by size-exclusion chromatography (SEC). Only PMMA of lowest molar mass was preferentially solvated by epoxy but at low concentrations of epoxy in the mixture. At higher epoxy content PMMA was preferentially solvated by THF. A simultaneous and competitive solvation between the specific interactions PMMA-epoxy and the self association of epoxy at high concentrations would be the responsible of this inversion point. The more compacted coil of PMMA of higher molecular weights in solution could explain the lack of interaction of these po…

Chemical PhenomenaSize-exclusion chromatographymacromolecular substancesBiochemistryAnalytical ChemistryGel permeation chromatographychemistry.chemical_compoundPolymer chemistryPolymethyl MethacrylateBenzhydryl CompoundsMethyl methacrylateFuransBisphenol A diglycidyl etherTetrahydrofuranChromatographyMolar massChemistry PhysicalOrganic Chemistrytechnology industry and agricultureGeneral MedicineEpoxyequipment and suppliesPoly(methyl methacrylate)Molecular Weightbody regionsSolubilitychemistryvisual_artCalibrationChromatography Gelvisual_art.visual_art_mediumEpoxy CompoundsAlgorithmsJournal of Chromatography
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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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