Search results for "acrylamide"

showing 10 items of 485 documents

Recombinant expression, in vitro refolding, and biophysical characterization of the N-terminal domain of T1R3 taste receptor

2012

Facteur d'impact (5 ans) : 1,617Notoriété à 2 ans : Acceptable (biochem.res.methods); The sweet taste receptor is a heterodimeric receptor composed of the T1R2 and T1R3 subunits, while T1R1 and T1R3 assemble to form the umami taste receptor. T1R receptors belong to the family of class C G-protein coupled receptors (GPCRs). In addition to a transmembrane heptahelical domain, class C GPCRs have a large extracellular N-terminal domain (NTD), which is the primary ligand-binding site. The T1R2 and T1R1 subunits have been shown to be responsible for ligand binding, via their NTDs. However, little is known about the contribution of T1R3-NTD to receptor functions. To enable biophysical characteriza…

TASTE RECEPTORSucroseCircular dichroismcongenital hereditary and neonatal diseases and abnormalitiesProtein Conformation[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionumami receptorUmamiSWEETENERmedicine.disease_causeReceptors G-Protein-Coupledtaste03 medical and health sciencesGPCRTaste receptorPROTEIN REFOLDINGexpressionEscherichia colimedicineHumansRECOMBINANT GPCRbacteriaReceptorEscherichia coli030304 developmental biologyG protein-coupled receptorInclusion Bodies0303 health sciencesChemistrysweet receptor030302 biochemistry & molecular biologyRecombinant ProteinsTransmembrane proteinnervous system diseasesResearch NoteBACTERIAL EXPRESSIONBiochemistrysugarElectrophoresis Polyacrylamide GelHeterologous expression[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionrecombinant proteinProtein BindingBiotechnology
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Thermal Denaturation of Pea Globulins (Pisum sativum L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation

2013

The heat-induced denaturation and aggregation of mixed pea globulins (8%, w/w) were investigated using differential scanning calorimetry (DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC). DSC data showed that the pea proteins denaturation temperature (T(d)) was heating-rate dependent. The T(d) value decreased by about 4 °C by lowering the heating rate from 10 to 5 °C/min. The SDS-PAGE analysis revealed that protein denaturation upon heating at 90 °C was mainly governed by noncovalent interaction. The SEC-HPLC measurements indicated that low-denatured legumin (≈350-410 kDa) and vicilin/convicilin (≈170 kDa) globulins were heat-denatured and most of their subunits reassociated int…

Thermal denaturationProtein DenaturationHot TemperatureChromatographyCalorimetry Differential ScanningbiologyGlobulinProtein ConformationChemistryPeasfood and beveragesGlobulinsGeneral ChemistryProtein aggregationbiology.organism_classificationPisumSativumDifferential scanning calorimetrybiology.proteinLeguminElectrophoresis Polyacrylamide GelDenaturation (biochemistry)General Agricultural and Biological SciencesPlant ProteinsJournal of Agricultural and Food Chemistry
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Cultured Ito cells of rat liver express the alpha 2-macroglobulin gene.

1987

Ito cells were isolated from rat liver and kept in culture for up to 13 days. The capability of the Ito cells to synthesize a2-macroglobulin was analyzed at different times after isolation and by pulse-chase experiments. Newly synthesized a2-macroglobulin was determined by immunoprecipitation followed by sodium dodecyl sulfate/ polyacrylamide gel electrophoresis and fluorography. a2-Macroglobulin synthesis was hardly detectable in Ito cells and their media 3 days after plating. However, 5 - 11 days after the isolation of the cells, increasing amounts of a2-macroglobulin were synthesized. The results of pulse-chase experiments performed on day 7 showed that radioactively labeled a2-macroglob…

Time FactorsBiologydigestive systemBiochemistrychemistry.chemical_compoundfluids and secretionsAnimalsalpha-MacroglobulinsNorthern blotRNA MessengerSodium dodecyl sulfatePancreatic elastasePolyacrylamide gel electrophoresisCells CulturedImmunoassayDNALipid MetabolismMolecular biologyMacroglobulinRatsSecretory proteinPerisinusoidal spaceBiochemistrychemistryGene Expression RegulationLiverHepatic stellate cellElectrophoresis Polyacrylamide GelFemalecirculatory and respiratory physiologyEuropean journal of biochemistry
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Initial steps of wall protoplast regeneration in Candida albicans

1997

Summary Cell wall regeneration of individual Candida albicans yeast and mycelial protoplasts was studied with confocal and electron microscopy using polyclonal antibodies and leetins. Quantitative measurements of the fluorescence emitted by individual protoplasts during the process of regeneration indicate that chitin is the first polymer to be laid down, whereas β(1,3)- and β(1,6)glucan are incorporated at a later stage. Mannoproteins were found on the surface of fresh protoplasts and those newly synthesized were then deposited with time. During the first steps of wall regeneration, the proteins that interacted covalently with chitin or glucan were different, but the same species were foun…

Time FactorsBlotting WesternChitinMicrobiologyMicrobiologyFungal ProteinsCell wallchemistry.chemical_compoundChitinCell WallCandida albicansCell Wall SkeletonFluorescent Antibody Technique IndirectCandida albicansGlucansMolecular BiologyGlucanchemistry.chemical_classificationMembrane GlycoproteinsbiologyProtoplastsRegeneration (biology)fungiGeneral MedicineProtoplastbiology.organism_classificationYeastcarbohydrates (lipids)Microscopy ElectronBiochemistrychemistryPolyclonal antibodiesbiology.proteinElectrophoresis Polyacrylamide GelCell DivisionResearch in Microbiology
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72/74As-labeling of HPMA based polymers for long-term in vivo PET imaging

2010

Abstract In the context of molecular imaging, various polymers based on the clinically approved N-(2-hydroxypropyl)-methacrylamide (HPMA) have been radio-labeled using longer-living positron emitters 72As t1/2 = 26 h or 74As t1/2 = 17.8 d. This approach may lead to non-invasive determination of the long-term in vivo fate of polymers by PET (positron emission tomography). Presumably, the radio label itself will not strongly influence the polymer structure due to the fact that the used nuclide binds to already existing thiol moieties within the polymer structure. Thus, the use of additional charges or bulky groups can be avoided.

Time FactorsClinical BiochemistryPharmaceutical ScienceContext (language use)BiochemistryArsenicIn vivoDrug DiscoveryPolymer chemistrymedicineMolecular BiologyRadioisotopeschemistry.chemical_classificationAcrylamidesmedicine.diagnostic_testOrganic ChemistryArsenic isotopePositron emittersPolymerPet imagingchemistryPositron emission tomographyPositron-Emission TomographyBiophysicsMolecular MedicineMolecular imagingBioorganic & Medicinal Chemistry Letters
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Is tubulin the sole antigen recognized by a putative anti-bursicon antibody?

1999

Abstract A 56-kDa polypeptide suspected to be the tanning hormone `bursicon' was analyzed using the monoclonal antibody (mAb) 01C10 of Song and Ma. We studied the beetle Tenebrio molitor, for which data on bursicon have been recently published. After purification by two-dimensional gel electrophoresis of brain proteins, the immunoreactive 56-kDa polypeptide was trypsinated and microsequenced. The obtained sequences revealed a high homology with α- and β-tubulins. In a complementary study, immunoreactive clones were isolated, using the 01C10 mAb, from a library in expression vector obtained from Drosophila melanogaster head cDNAs. Again, the isolated clones were found, after cDNA sequencing,…

Time FactorsInvertebrate HormonesPhysiologymedicine.drug_classBlotting WesternAntibody AffinityEnzyme-Linked Immunosorbent AssayMonoclonal antibodyBiochemistryAntigenTubulinImmunoscreeningmedicineAnimalsTenebrioMolecular BiologyCells CulturedChromatography High Pressure LiquidBursiconGene LibraryGel electrophoresisExpression vectorbiologyAntibodies MonoclonalBrainSequence Analysis DNAMolecular biologyTubulinbiology.proteinChromatography GelDrosophilaElectrophoresis Polyacrylamide GelAntibodyComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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The Effect of Long-Term Storage on the Biological and Histological Properties of Cryopreserved Amniotic Membrane

2011

Cryopreserved amniotic membrane (AM) is widely used in ophthalmology because of its anti-angiogenic, anti-inflammatory, and wound healing promoting capabilities. A common method to conserve the tissue is the storage in cryo-medium containing 50% glycerol at -80°C. The aim of this study was to examine the influence of storage time on the sterility as well as the histological and biological properties of cryopreserved AM.Amniotic membrane from different donors was stored in cell culture media containing 50% glycerol for different time periods, on average 4 months (group 1), 15 months (group 2), and 24 months (group 3), at -80°C. Samples of the tissue and cryo-medium were examined for bacteria…

Time FactorsSterilityBlotting WesternOrgan Preservation SolutionsMedizinTissue BanksBiologyCryopreservationAndrologyCellular and Molecular Neurosciencechemistry.chemical_compoundGlycerolHumansAmnionPolyacrylamide gel electrophoresisCryopreservationExtracellular Matrix ProteinsBacteriaBiological DressingsFungiOrgan PreservationSensory SystemsCulture MediaBlotOphthalmologyMembranechemistryTissue bankImmunologyCytokinesElectrophoresis Polyacrylamide GelWound healingBiomarkersCurrent Eye Research
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Acrylamide catalytically inhibits topoisomerase II in V79 cells.

2010

The vinyl monomer acrylamide is characterized by the presence of an alpha,beta-unsaturated carbonyl group that makes it reactive towards thiol, hydroxyl or amino groups and towards the nucleophilic centers in DNA. The ability of acrylamide to chemically modify protein thiols has prompted us to consider topoisomerase II as one possible target of acrylamide, since agents targeting protein sulfhydryl groups act as either catalytic inhibitors or poisons of topoisomerase II. Nuclear extracts from V79 Chinese hamster cells incubated with acrylamide reduced topoisomerase II activity as inferred by an inability to convert kinetoplast DNA to the decatenated form. Nuclear extracts incubated with acry…

ToxicologyCleavage (embryo)Cell LineColony-Forming Units AssayV79 cellchemistry.chemical_compoundCell Line TumorCricetinaemedicineAnimalsTopoisomerase II InhibitorsDNA CleavageEtoposideEtoposideNucleic Acid Synthesis Inhibitorschemistry.chemical_classificationCell NucleusAcrylamidebiologyTopoisomeraseDNA KinetoplastGeneral MedicineTopoisomerase IIAntineoplastic Agents PhytogenicSettore BIO/18 - GeneticaEnzymechemistryBiochemistryKinetoplastAcrylamidebiology.proteinTopoisomerase-II InhibitorDNAmedicine.drugToxicology in vitro : an international journal published in association with BIBRA
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Preparation of electrophoretic variants of Corticosteroid-binding Globulin (CBG) using liquid liquid partition chromatography

1988

Abstract Human corticosteroid-binding globulin (CBG) was purified to homogeneity by application of three different chromatographic methods. After fractionation of pregnancy serum with ammonium sulfate the 80%-pellet was used for affinity chromatography based on tresyl activated Sepharose (Pharmacia, Uppsala, Sweden). The affinity eluate was injected into a Mono Q anion exchange column (Pharmacia). Fractions containing CBG were finally purified by liquid liquid chromatography on LiParGel 750 (Merck, Darmstadt, F.R.G.) 1,2 . The purified protein was characterized by IEF and PAGE. This paper describes a method for the chromatographic separation of the two variants of CBG without a loss of bind…

TranscortinPharmacologyAmmonium sulfateChromatographybiologyGlobulinChemistryElutionOrganic ChemistryClinical BiochemistryFractionationBiochemistryChromatography AffinitySepharoseElectrophoresischemistry.chemical_compoundEndocrinologyTranscortinAffinity chromatographybiology.proteinHumansElectrophoresis Polyacrylamide GelMolecular BiologyChromatography LiquidSteroids
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Molecular characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum: gene cloning, transcriptional analysis, overex…

1997

By using degenerate primers designed from the first 19 N-terminal amino acids of Lactobacillus plantarum p-coumaric acid decarboxylase (PDC), a 56-bp fragment was amplified from L. plantarum in PCRs and used as a probe for screening an L. plantarum genomic bank. Of the 2,880 clones in the genomic bank, one was isolated by colony hybridization and contained a 519-bp open reading frame (pdc gene) followed by a putative terminator structure. The pdc gene is expressed on a monocistronic transcriptional unit, which is transcribed from promoter sequences homologous to Lactococcus promoter sequences. No mRNA from pdc and no PDC activity were detected in uninduced cell extracts, indicating that the…

Transcription GeneticCarboxy-LyasesMolecular Sequence Datamacromolecular substancesMolecular cloningmedicine.disease_causePolymerase Chain ReactionApplied Microbiology and BiotechnologyOpen Reading FramesLactococcusGene expressionEscherichia colimedicineGenomic libraryAmino Acid SequenceCloning MolecularPromoter Regions GeneticEscherichia coliGeneGene LibraryRecombination GeneticElectronic Data ProcessingBase SequenceEcologybiologyNucleic acid sequenceChromosome MappingNucleic Acid Hybridizationhemic and immune systemsGene Expression Regulation BacterialBlotting Northernbiology.organism_classificationMolecular biologyRecombinant ProteinsBlotting SouthernLactobacillusRNA BacterialTerminator (genetics)BiochemistryEnzyme InductionElectrophoresis Polyacrylamide GelLactobacillus plantarumResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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