Search results for "recombinant"

showing 10 items of 1150 documents

Single Molecule Spectroscopy of Oriented Recombinant Trimeric Light Harvesting Complexes of Higher Plants

2002

The bleaching dynamics of reconstituted single light-harvesting chlorophyll a/b investigated. The complexes containing one histidine6 tag per monomeric subunit were immobilised predominantly in a defined orientation with their symmetry axis perpendicular to a Ni-ion-containing surface allowing for the first time the examination of single LHCIIb in an aqueous environment. Most complexes exhibit photobleaching in one step, indicating coupling between the monomeric subunits leading to an energy transfer between adjacent subunits. Differences in bleaching behaviour between these and previous observations with single LHCIIb are discussed.

Aqueous solutionProtein subunitClinical BiochemistryGeneral ChemistryPhotochemistryPhotobleachingGeneral Biochemistry Genetics and Molecular BiologySingle Molecule Spectroscopylaw.inventionLight-harvesting complexCoupling (electronics)chemistry.chemical_compoundCrystallographyMonomerchemistrylawRecombinant DNAMolecular BiologySingle Molecules
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INFγ stimulates arginine transport through system y+L in human monocytes

2004

Freshly isolated human monocytes transport L-arginine mostly through a sodium independent, NEM insensitive pathway inhibited by L-leucine in the presence, but not in the absence of sodium. Interferon-gamma (IFNgamma) stimulates this pathway, identifiable with system y+L, and markedly enhances the expression of SLC7A7, the gene that encodes for system y+L subunit y+LAT1, but not of SLC7A6, that codes for the alternative subunit y+LAT2. System y+ plays a minor role in arginine uptake by monocytes and the expression of system y+-related genes, SLC7A1 and SLC7A2, is not changed by IFNgamma. These results demonstrate that system y+L is sensitive to IFNgamma.

ArginineSodiumProtein subunitBiophysicschemistry.chemical_elementBiologyLPI - Lysinuric protein intoleranceArginineMonocyteBiochemistryMonocytesInterferon-gammaInterferon γLeucineStructural BiologyArginine transportSystem y+L.GeneticsmedicineHumansMolecular BiologyGeneLysinuric protein intoleranceCells CulturedArginine transportReverse Transcriptase Polymerase Chain ReactionFusion Regulatory Protein 1 Light ChainsMonocyteSodiumAmino Acid Transport System y+LBiological TransportCell BiologyMolecular biologyRecombinant ProteinsKineticsmedicine.anatomical_structurechemistryEthylmaleimideAmino Acid Transport Systems BasicInterferon-γFEBS Letters
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Enzyme replacement therapy for mucopolysaccharidosis VI: evaluation of long-term pulmonary function in patients treated with recombinant human N-acet…

2010

Pulmonary function is impaired in untreated mucopolysaccharidosis type VI (MPS VI). Pulmonary function was studied in patients during long-term enzyme replacement therapy (ERT) with recombinant human arylsulfatase B (rhASB; rhN-acetylgalactosamine 4-sulfatase). Pulmonary function tests prior to and for up to 240 weeks of weekly infusions of rhASB at 1 mg/kg were completed in 56 patients during Phase 1/2, Phase 2, Phase 3 and Phase 3 Extension trials of rhASB and the Survey Study. Forced vital capacity (FVC), forced expiratory volume in 1 s (FEV1) and, in a subset of patients, maximum voluntary ventilation (MVV), were analyzed as absolute volume in liters. FEV1 and FVC showed little change f…

Arylsulfatase BAdultmedicine.medical_specialtyVital capacityAdolescentMucopolysaccharidoses (MPS)N-Acetylgalactosamine-4-SulfataseMucopolysaccharidosis type VIClinical SciencesUrologyPulmonary function testingPlacebos03 medical and health sciencesFEV1/FVC ratio0302 clinical medicineRare DiseasesDouble-Blind MethodClinical ResearchmedicineGeneticsHumansGenetics(clinical)Longitudinal StudiesChildPreschoolLungGenetics (clinical)Genetics & Heredity0303 health sciencesLungMucopolysaccharidosis VIbusiness.industry030305 genetics & heredityEvaluation of treatments and therapeutic interventionsMucopolysaccharidosis VIEnzyme replacement therapyRecombinant Proteins3. Good healthSurgeryRespiratory Function Testsmedicine.anatomical_structureCross-Sectional StudiesResearch DesignChild Preschool6.1 PharmaceuticalsOriginal Articlebusiness030217 neurology & neurosurgery
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Receptor phosphorylation does not mediate cross talk between muscarinic M(3) and bradykinin B(2) receptors.

1999

This study examined cross talk between phospholipase C-coupled muscarinic M3and bradykinin B2receptors coexpressed in Chinese hamster ovary (CHO) cells. Agonists of either receptor enhanced phosphoinositide signaling (which rapidly desensitized) and caused protein kinase C (PKC)-independent, homologous receptor phosphorylation. Muscarinic M3but not bradykinin B2receptors were also phosphorylated after phorbol ester activation of PKC. Consistent with this, muscarinic M3receptors were phosphorylated in a PKC-dependent fashion after bradykinin B2receptor activation, but muscarinic M3receptor activation did not influence bradykinin B2receptor phosphorylation. Despite heterologous phosphorylatio…

Atropinemedicine.medical_specialtyReceptor Bradykinin B2PhysiologyGene ExpressionCHO CellsInositol 145-TrisphosphateMuscarinic AntagonistsBiologyMuscarinic AgonistsBradykininTransfectionTritiumInternal medicineCricetinaeMuscarinic acetylcholine receptor M5Muscarinic acetylcholine receptormedicineMuscarinic acetylcholine receptor M4AnimalsHumansBradykinin receptorPhosphorylationReceptorMethacholine ChlorideReceptor Muscarinic M3Receptors BradykininMuscarinic acetylcholine receptor M3Muscarinic acetylcholine receptor M2Cell BiologyMuscarinic acetylcholine receptor M1Receptor Cross-TalkReceptors MuscarinicRecombinant ProteinsEndocrinologyType C PhospholipasesCalciumInositolSignal TransductionThe American journal of physiology
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Clathrin-mediated constitutive endocytosis of PIN auxin efflux carriers in Arabidopsis.

2007

SummaryEndocytosis is an essential process by which eukaryotic cells internalize exogenous material or regulate signaling at the cell surface [1]. Different endocytic pathways are well established in yeast and animals; prominent among them is clathrin-dependent endocytosis [2, 3]. In plants, endocytosis is poorly defined, and no molecular mechanism for cargo internalization has been demonstrated so far [4, 5], although the internalization of receptor-ligand complexes at the plant plasma membrane has recently been shown [6]. Here we demonstrate by means of a green-to-red photoconvertible fluorescent reporter, EosFP [7], the constitutive endocytosis of PIN auxin efflux carriers [8] and their …

Auxin effluxmedia_common.quotation_subjectRecombinant Fusion ProteinseducationEndocytic cycleArabidopsisBiologyEndocytosisClathrinPlant RootsGeneral Biochemistry Genetics and Molecular BiologyExocytosisGenes ReporterPIN proteinsInternalizationmedia_commonAgricultural and Biological Sciences(all)Indoleacetic AcidsBiochemistry Genetics and Molecular Biology(all)Arabidopsis ProteinsProtoplastsCell MembraneClathrin-Coated VesiclesReceptor-mediated endocytosisClathrinEndocytosisCell biologyLuminescent Proteinsbiology.proteinCELLBIOGeneral Agricultural and Biological SciencesCurrent biology : CB
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Autoimmunity seen through the SEREX-scope.

2003

Autoantibodies can be detected in autoimmune diseases with a long prodromal phase and may serve as early indicators of disease activity. Autoantibody-based screening methods are therefore potent tools for the identification of target antigens. The SEREX method (serological identification of antigens by recombinant expression cloning) has been developed for the serological definition of immunogenic tumor antigens. Recent studies indicate that the SEREX approach may also be utilized for the analysis of complex immune responses involved in autoimmune diseases.

B-LymphocytesRecombinant expressionImmunologyAutoantibodyAutoimmunityBiologymedicine.disease_causeRecombinant ProteinsAutoimmunitySerologyAutoimmune DiseasesMiceImmune systemImmunizationAntigenImmunologyScreening methodmedicineImmunology and AllergyAnimalsHumansImmunizationSerologic TestsAutoantibodiesAutoimmunity reviews
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Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment.

2006

Abstract In an attempt to directly approach the postulated toxic domain of Clostridium difficile 's TcdB-10463, eight subclones of different size and locations in the N-terminal third of the toxin were generated. Expression of these toxin fragments was checked in Western blots and the enzymatic activity of the expressed proteins was analyzed by glucosylating Ras related small GTP-binding proteins. Two polypeptides of 875 aa (TcdBc1–3) and 557 aa (TcdBc1-H) glucosylated their targets Rho, Rac and Cdc42 with the same activity and specificity as the holotoxin. In comparison 516 aa (TcdBc1-N) and 467 aa (TcdBc1-A) protein fragments exhibited highly reduced activity, while Tcdc1 and TcdB2–3 (aa …

Bacterial ToxinsMolecular Sequence DataClostridium difficile toxin Bmedicine.disease_causeMicrobiologyStructure-Activity RelationshipGTP-binding protein regulatorsClostridiumBacterial ProteinsGeneticsmedicineMolecular Biologychemistry.chemical_classificationBinding SitesbiologyBase SequenceToxinbiology.organism_classificationMolecular biologyPeptide FragmentsRecombinant ProteinsAmino acidEnzymechemistryCdc42 GTP-Binding ProteinBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseFEMS microbiology letters
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Bioencapsulation of living bacteria (Escherichia coli) with poly(silicate) after transformation with silicatein-α gene

2007

Bioencapsulation is an intriguing way to immobilize biological materials, including cells, in silica, metal-oxides or hybrid sol-gel polymers. Until now only the sol-gel precursor technology was utilized to immobilize bacteria or yeast cells in silica. With the discovery of silicatein, an enzyme from demosponges that catalyzes the formation of poly(silicate), it became possible to synthesize poly(silicate) under physiological (ambient) conditions. Here we show that Escherichia coli can be transformed with the silicatein gene, its expression level in the presence of isopropyl beta-D-thiogalactopyranoside (IPTG) can be efficiently intensified by co-incubation with silicic acid. This effect co…

Bacterial capsuleMaterials scienceBiophysicsGene Expressionlac operonBioengineeringmedicine.disease_causelaw.inventionBiomaterialschemistry.chemical_compoundlawEscherichia colimedicineTransgenesSilicic acidEscherichia coliBacterial Capsuleschemistry.chemical_classificationMicrobial ViabilitybiologySilicatesSodiumbiology.organism_classificationCathepsinsYeastEnzymechemistryBiochemistryMechanics of MaterialsMicroscopy Electron ScanningCeramics and CompositesRecombinant DNABacteriaBiomaterials
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Purification and analysis of polyhistidine-tagged human parvovirus B19 VP1 and VP2 expressed in insect cells

2008

Human parvovirus B19 is an autonomously replicating human pathogen with a specific tropism for human erythroid progenitor cells. There is an interest in producing empty nucleocapsids of B19 as they can be used as tools in molecular biology and diagnostics. Native B19 virus particles are formed from two structural viral proteins, VP1 and VP2. The VP2 protein alone is able to self assemble and consequently form virus-like particles (VLPs) in heterologous expression systems. Purification of recombinant VLPs has been conducted using various traditional methods. These include laborious and time-consuming, e.g. cesium chloride or sucrose gradient ultracentrifugation steps, allowing limited workin…

BaculoviridaeInsectavirusesCell Linelaw.invention03 medical and health scienceschemistry.chemical_compoundAffinity chromatographylawVirologyParvovirus B19 HumanAnimalsHumansHistidinePolyhistidine-tag030304 developmental biologyErythroid Precursor Cells0303 health sciencesbiology030306 microbiologyVirionvirus diseasesbiochemical phenomena metabolism and nutritionbiology.organism_classificationFusion proteinMolecular biologyRecombinant ProteinsGene Expression RegulationCapsidchemistryBiochemistryRecombinant DNACapsid ProteinsUltracentrifugeHeterologous expressionJournal of Virological Methods
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Generation of lentivirus vectors using recombinant baculoviruses

2008

In spite of advances in conventional four-plasmid transient transfection methods and development of inducible stable production cell lines, production of replication-defective lentiviral vectors in clinical scale has been challenging. Baculovirus technology offers an alternative to scalable virus production as a result of fast and easy production of baculoviruses, efficient transduction of mammalian cells and safety of the baculoviruses. As a first step toward scalable lentiviral production system, we have constructed four recombinant baculoviruses: the BAC-transfer virus expresses green fluorescent protein (GFP) as a transgene and BAC-gag-pol, BAC-vesicular stomatitis virus glycoprotein G …

BaculoviridaevirusesGenetic enhancementGenetic VectorsGreen Fluorescent ProteinsGene ExpressionVirus ReplicationCell LineGreen fluorescent proteinlaw.inventionTransduction (genetics)Transduction GeneticlawVirologyGeneticsHumansTransgenesCloning MolecularMolecular BiologyOrganisms Genetically ModifiedbiologyLentivirusGenetic TherapyFlow Cytometrybiology.organism_classificationVirologyMicroscopy FluorescenceViral replicationCell cultureLentivirusRecombinant DNAMolecular MedicineBaculoviridaeHeLa CellsGene Therapy
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