Search results for "Poly(acrylamide)"

showing 10 items of 377 documents

Recombinant laccase from Pediococcus acidilactici CECT 5930 with ability to degrade tyramine

2017

Biogenic amines degradation by bacterial laccases is little known, so we have cloned and heterologously expressed, in E. coli, a new laccase from Pediococcus acidilactici CECT 5930 (Lpa5930), a lactic acid bacterium commonly found in foods able to degrade tyramine. The recombinant enzyme has been characterized by physical and biochemical assays. Here we report the optimization of expression and purification procedures of this laccase. DNA encoding sequence of laccase from P. acidilactici was amplified by PCR and cloned into the expression plasmid pET28a for induction by isopropyl-β-D-thiogalactoipyranoside. Protein expression was performed in E. coli BL21(DE3) harboring pGro7 plasmid expres…

0106 biological sciences0301 basic medicineArabinoseMolecular biologylcsh:MedicineLaccasesBiochemistryBiotecnologia01 natural sciencesSubstrate Specificitylaw.inventionDatabase and Informatics Methodschemistry.chemical_compoundlawRecombinant Protein PurificationCloning MolecularAmineslcsh:Sciencechemistry.chemical_classificationMultidisciplinaryABTSbiologyOrganic CompoundsTemperatureHydrogen-Ion ConcentrationTyramineRecombinant ProteinsEnzymesChemistryRecombination-Based AssayBiochemistryPhysical SciencesRecombinant DNAElectrophoresis Polyacrylamide GelOxidation-ReductionSequence AnalysisResearch ArticleProtein PurificationBioinformaticsTyramineLibrary ScreeningDNA constructionResearch and Analysis Methods03 medical and health sciencesBacterial ProteinsSequence Motif Analysis010608 biotechnologyAmino Acid SequenceBenzothiazolesPediococcus acidilacticiLaccaseMolecular Biology Assays and Analysis TechniquesBase SequenceMolecular massLaccaseOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsPediococcus acidilacticiSequence Analysis DNAbiology.organism_classificationMolecular biology techniques030104 developmental biologyEnzymechemistryPlasmid ConstructionEnzymologySpectrophotometry Ultravioletlcsh:QSulfonic AcidsEnzimsProteïnesPurification TechniquesPLOS ONE
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The shell matrix of the pulmonate land snail Helix aspersa maxima.

2012

12 pages; International audience; In mollusks, the shell mineralization process is controlled by an array of proteins, glycoproteins and polysaccharides that collectively constitute the shell matrix. In spite of numerous researches, the shell protein content of a limited number of model species has been investigated. This paper presents biochemical data on the common edible land snail Helix aspersa maxima, a model organism for ecotoxicological purposes, which has however been poorly investigated from a biomineralization viewpoint. The shell matrix of this species was extracted and analyzed biochemically for functional in vitro inhibition assay, for amino acid and monosaccharides composition…

0106 biological sciencesBiomineralizationPulmonate snailPhysiology01 natural sciencesBiochemistryMineralization (biology)chemistry.chemical_compoundX-Ray DiffractionTandem Mass SpectrometryElectrophoresis Gel Two-DimensionalHaliotisAmino AcidsComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesEcologyMonosaccharidesLand snailImmunogold labellingImmunohistochemistryAmino acidBiochemistryElectrophoresis Polyacrylamide GelTerrestrial snail ; biomineralization ; shell ; aragonite ; crossed-lamellar ; protein ; immunogold ; gel electrophoresisFrancefood.ingredientBiology010603 evolutionary biologyCalcium Carbonate03 medical and health sciencesfoodSpecies SpecificityAnimal ShellsShellAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biology030304 developmental biologyHelix SnailsProteinsCrossed-lamellarbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsGel electrophoresis[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyCalcium carbonatechemistryMicroscopy Electron ScanningBiomineralizationPinctadaComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the correspondi…

1997

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 4…

0106 biological sciencesDNA ComplementaryMolecular Sequence DataBiology4-Hydroxyphenylpyruvate Dioxygenase01 natural sciencesBiochemistry03 medical and health sciencesDioxygenaseComplementary DNA[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biologyHomogentisate 12-dioxygenase0303 health sciencesBase SequenceSequence Homology Amino AcidMolecular massDioxygenase activityNucleic acid sequenceCell BiologyMolecular biologyDaucus carotaBiochemistryElectrophoresis Polyacrylamide Gel4-Hydroxyphenylpyruvate dioxygenaseResearch ArticleChromatography LiquidSubcellular Fractions010606 plant biology & botany
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Impact of Pressurized Liquid Extraction and pH on Protein Yield, Changes in Molecular Size Distribution and Antioxidant Compounds Recovery from Spiru…

2021

The research aims to extract nutrients and bioactive compounds from spirulina using a non-toxic, environmentally friendly and efficient method—Pressurized Liquid Extraction (PLE). In this work, Response Surface Methodology (RSM)–Central Composite Design (CCD) was used to evaluate and optimize the extraction time (5–15 min), temperature (20–60 °C) and pH (4–10) during PLE extraction (103.4 bars). The multi-factor optimization results of the RSM-CCD showed that under the pressure of 103.4 bars, the optimal conditions to recover the highest content of bioactive compounds were 10 min, 40 °C and pH 4. Furthermore, the compounds and antioxidant capacity of PLE and non-pressurized extraction extra…

0106 biological sciencesHealth (social science)AntioxidantPLEmedicine.medical_treatmentTP1-1185Plant Science01 natural sciencesHealth Professions (miscellaneous)MicrobiologyArticleCinnamic acidchemistry.chemical_compoundTriple TOF–LC–MS–MS0404 agricultural biotechnology010608 biotechnologymedicineResponse surface methodologySodium dodecyl sulfatePolyacrylamide gel electrophoresisCarotenoidRSM-CCDchemistry.chemical_classificationbioactive compoundsChromatographyChemical technologymicroalgaeExtraction (chemistry)04 agricultural and veterinary sciences040401 food science6. Clean waterchemistryPolyphenolSDS-PAGEFood ScienceFoods
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Purification and characterization of geranyl diphosphate synthase from Vitis vinifera L. cv Muscat de Frontignant cell cultures

1993

A geranyl diphosphate synthase (EC 2.5.1.1), which catalyzes the formation of geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, was isolated from Vitis vinifera L. cv Muscat de Frontignan cell cultures. Purification of the enzyme was achieved successively by ammonium sulfate precipitation and chromatography on DEAE-Sephacel, hydroxylapatite, Mono Q, Phenyl Superose, Superose 12, and preparative nondenaturing polyacrylamide gels. The enzyme formed only geranyl diphosphate as a product. In all cases, neither neryl diphosphate, the cis isomer, nor farnesyl diphosphate was detected. The enzyme showed a native molecular mass of 68 [plus or minus] 5 kD as determined …

0106 biological sciencesPhysiologyStereochemistry[SDV]Life Sciences [q-bio]PolyacrylamidePlant Science01 natural sciencesCofactor[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compound[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsSodium dodecyl sulfateAmmonium sulfate precipitationComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyMolecular mass[SDV] Life Sciences [q-bio]EnzymechemistryCell cultureCULTURE DE CELLULEbiology.proteinCis–trans isomerism010606 plant biology & botanyResearch Article
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In vivoanalysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain

2007

International audience; The endoplasmic reticulum (ER) chaperone binding protein (BiP) binds exposed hydrophobic regions of misfolded proteins. Cycles of ATP hydrolysis and nucleotide exchange on the ATPase domain were shown to regulate the function of the ligand-binding domain in vitro. Here we show that ATPase mutants of BiP with defective ATP-hydrolysis (T46G) or ATP-binding (G235D) caused permanent association with a model ligand, but also interfered with the production of secretory, but not cytosolic, proteins in vivo. Furthermore, the negative effect of BiP(T46G) on secretory protein synthesis was rescued by increased levels of wild-type BiP, whereas the G235D mutation was dominant. U…

0106 biological sciencesgenetic structuresRecombinant Fusion ProteinsATPaseBlotting WesternGreen Fluorescent ProteinsPlant ScienceBINDING PROTEINEndoplasmic ReticulumModels Biological01 natural sciencesChromatography Affinity[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesAdenosine TriphosphateTobaccoPROTEIN FOLDINGGeneticsImmunoprecipitationEndoplasmic Reticulum Chaperone BiPHSP70Heat-Shock Proteins030304 developmental biologyCHAPERONEAdenosine Triphosphatases0303 health sciencesbiologyHydrolysisProtoplastsEndoplasmic reticulumBinding proteinCell BiologyPlants Genetically ModifiedLigand (biochemistry)Secretory proteinBiochemistryChaperone (protein)MutationChaperone bindingbiology.proteinATPASEElectrophoresis Polyacrylamide GelProtein foldingMolecular ChaperonesProtein BindingSignal Transduction010606 plant biology & botanyThe Plant Journal
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Analysis of the 3H8 antigen of Candida albicans reveals new aspects of the organization of fungal cell wall proteins.

2017

The walls of both, yeast and mycelial cells of Candida albicans possess a species-specific antigen that is recognized by a monoclonal antibody (MAb 3H8). This antigen can be extracted in the form of a very high Mr complex, close or over 106 Da, by treatment, with β-1,3-glucanase, β mercaptoethanol or dithothreitol, or mild alkali, but not by saturated hydrogen fluoride (HF) in pyridine, suggesting that the complex is bound to wall β-1,3 glucans, and to proteins by disulfide bonds, but not to β-1,6 glucans. Through its sensitivity to trypsin and different deglycosylation procedures, it was concluded that the epitope is associated to a glycoprotein containing N-glycosidic, but not O-glycosidi…

0301 basic medicineAntigens FungalMacromolecular SubstancesApplied Microbiology and BiotechnologyMicrobiologyEpitopeMass SpectrometryCell wall03 medical and health sciencesAntigenCell WallCandida albicansmedicineCandida albicansPolyacrylamide gel electrophoresisAntibodies FungalMannanchemistry.chemical_classificationbiologyAntibodies MonoclonalGeneral Medicinebiology.organism_classificationTrypsinMicroscopy Electron030104 developmental biologyBiochemistrychemistryElectrophoresis Polyacrylamide GelGlycoproteinmedicine.drugFEMS yeast research
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Staining SDS-PAGE gels of skeletal matrices after western blot: a way to improve their sharpness.

2015

7 pages; International audience; Denaturing 1D electrophoresis on acrylamide gels - also referred as SDS-PAGE - is a classical technique for fractionating and visualizing the macromolecular constituents of matrices associated to calcified tissues. This technique has been widely used in association with the subsequent silver nitrate staining. But because matrices associated to calcified tissues are very often glycosylated and constituted of numerous polydisperse macromolecules, the obtained pattern is frequently 'smeary' and discrete bands, when present on the gel, are often blurred, thickened or totally masked by the polydisperse macromolecules. In this paper, we present a simple protocol t…

0301 basic medicineChromatographymedicine.diagnostic_testMechanical EngineeringStaining03 medical and health sciencesElectrophoresischemistry.chemical_compoundSilver nitrate030104 developmental biologyMembranechemistryWestern blotMechanics of Materials[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Acrylamide[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]medicine[SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]General Materials SciencePolyacrylamide gel electrophoresisComputingMilieux_MISCELLANEOUSMacromolecule
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Zymography Methods to Simultaneously Analyze Superoxide Dismutase and Catalase Activities: Novel Application for Yeast Species Identification

2017

We provide an optimized protocol for a double staining technique to analyze superoxide dismutase enzymatic isoforms Cu-Zn SOD (Sod1) and Mn-SOD (Sod2) and catalase in the same polyacrylamide gel. The use of NaCN, which specifically inhibits yeast Sod1 isoform, allows the analysis of Sod2 isoform while the use of H2O2 allows the analysis of catalase. The identification of a different zymography profiling of SOD and catalase isoforms in different yeast species allowed us to propose this technique as a novel yeast identification and classification strategy.

0301 basic medicineGene isoformchemistry.chemical_classificationbiologySOD2Molecular biologyYeastSuperoxide dismutase03 medical and health sciences030104 developmental biology0302 clinical medicineEnzymechemistryCatalasebiology.proteinZymographyPolyacrylamide gel electrophoresis030217 neurology & neurosurgery
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Cytotoxic activity of Holothuria tubulosa (Echinodermata) coelomocytes.

2017

Abstract The immune system of marine invertebrates, in particular that of holothurians, still requires further study. Our research showed that coelomocyte cells contained in the coelomic fluid of the sea cucumber, Holothuria tubulosa, are able to lyse, in vitro, red blood cells in rabbits and sheep. A plaque-forming assay showed spherule cells to be the effector cells, able to release cytotoxic molecules after xenogenic cell contact. The coelomocyte lysate supernatant, analysed by polyacrylamide gel electrophoresis overlay technique, using rabbit and sheep erythrocytes, showed two different haemolytic protein patterns: one calcium dependent and the other calcium independent. The fractions o…

0301 basic medicineLysisErythrocytesOverlay assayAquatic ScienceMicrobiologyLysis plaque assay03 medical and health sciencesSea cucumber0302 clinical medicineImmune systemLeukocytesEnvironmental ChemistryCytotoxic T cellAnimalsHolothuriaPolyacrylamide gel electrophoresisCoelomocyteSheepbiologyHolothuria tubulosaGeneral Medicinebiology.organism_classificationHolothuria tubulosaIn vitroImmunity InnateHaemolytic activity030104 developmental biologyBiochemistryElectrophoresis Polyacrylamide GelCoelomocyteRabbits030215 immunologyFishshellfish immunology
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