Search results for "Purification Techniques"

showing 2 items of 2 documents

Comparison of hemolytic activity of the intermediate subunit of Entamoeba histolytica and Entamoeba dispar lectins.

2017

Galactose and N-acetyl-D-galactosamine-inhibitable lectin of Entamoeba histolytica has roles in pathogenicity and induction of protective immunity in rodent models of amoebiasis. Recently, the intermediate subunit of the lectin, Igl1, of E. histolytica has been shown to have hemolytic activity. However, the corresponding lectin is also expressed in a non-virulent species, Entamoeba dispar, and another subunit, Igl2, is expressed in the protozoa. Therefore, in this study, we compared the activities of Igl1 and Igl2 subunits from E. histolytica and E. dispar using various regions of recombinant Igl proteins expressed in Escherichia coli. The recombinant E. dispar Igl proteins had comparable h…

0301 basic medicineErythrocytesTime Factorslcsh:MedicineProtein Sequencingmedicine.disease_causePathology and Laboratory MedicineBiochemistrylaw.inventionEntamoebafluids and secretionslawLectinsMedicine and Health SciencesRecombinant Protein Purificationlcsh:ScienceProtozoansMultidisciplinarybiologyPseudomonas AeruginosaRecombinant ProteinsBacterial PathogensMedical MicrobiologyRecombinant DNAPathogensResearch ArticleProtein PurificationProtein subunitDisparResearch and Analysis MethodsReal-Time Polymerase Chain ReactionMicrobiologyHemolysisMicrobiologyEntamoeba Histolytica03 medical and health sciencesEntamoeba histolyticaPseudomonasParasite Groupsparasitic diseasesmedicineAnimalsTrophozoitesHemoglobinGene SilencingHorsesMolecular Biology TechniquesSequencing TechniquesEscherichia coliMolecular BiologyMicrobial PathogensBacterialcsh:REntamoebaOrganismsLectinBiology and Life SciencesProteinsbiology.organism_classificationParasitic Protozoansdigestive system diseasesProtein Subunits030104 developmental biologybiology.proteinProtozoaParasitologylcsh:QApicomplexaPurification TechniquesPLoS ONE
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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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