Search results for "blotting"

showing 10 items of 899 documents

Taste, movement, and death: varying effects of new prospero mutants during Drosophila development

2003

0022-3034 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't; The PGal4 transposon inserted upstream of the pan-neural gene prospero (pros) causes several neural and behavioral defects in the Voila(1) strain. The precise excision of the transposon simultaneously rescued all these defects whereas its unprecise excision created new pros(V) alleles, including the null allele pros(V17). Here, we describe the relationship between the genetic structure of pros locus, larval locomotion, and larval gustatory response. These two behaviors showed varying degrees of variation depending upon the pros allele. We also found a good relation between behavioral alteration, the level …

GenotypeNerve Tissue Proteins/*genetics/metabolismeducationLethalMovement/*physiologyTaste/*geneticsDrosophila melanogaster/embryology/genetics/growth & developmentReaction TimeAnimalsDrosophila ProteinsNeuromuscular Junction/genetics/growth & development/metabolismSouthernLarva/genetics/*growth & developmentAllelesNonmammalianNuclear Proteins/*genetics/metabolismBlottingDevelopmental/physiologyImmunohistochemistryhumanitiesGenomics/methodsDeathInvertebrate/chemistryGene Expression RegulationGenesEmbryoMutationDNA Transposable ElementsGangliaInsectTranscription Factors
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Neuronal Cell Nuclear Factor. A Nuclear Receptor Possibly Involved in the Control of Neurogenesis and Neuronal Differentiation

1997

We have cloned from a cDNA library of neuronal derivatives of retinoic-acid-induced embryonic carcinoma cells a nuclear receptor that may be involved in the control of late neurogenesis and early neuronal differentiation. The receptor which is practically identical in sequence with germ cell nuclear factor, has been designated neuronal cell nuclear factor (NCNF). NCNF is exclusively expressed in the neuronal derivatives of PCC7-Mz1 cells, with the expression beginning within hours of exposure to retinoic acid. In the developing mouse brain, NCNF is expressed in the marginal zones of the neuroepithelium which are known to contain young postmitotic neurons. NCNF binds to the DRO sequence ther…

Germ cell nuclear factorRetinoic acidReceptors Cytoplasmic and NuclearTretinoinBiologyLigandsBiochemistryMicechemistry.chemical_compoundNuclear Receptor Subfamily 6 Group A Member 1Tumor Cells CulturedAnimalsCloning MolecularReceptorIn Situ HybridizationNuclear receptor co-repressor 1NeuronsNeurogenesisBrainGene Expression Regulation DevelopmentalCell DifferentiationDNABlotting NorthernMolecular biologyDNA-Binding ProteinsRepressor ProteinsNeuroepithelial cellNuclear receptor coactivator 1Blotting SouthernOligodeoxyribonucleotidesnervous systemchemistryNuclear receptorEuropean Journal of Biochemistry
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Stress-70 proteins in marine mussel Mytilus galloprovincialis as biomarkers of environmental pollution: a field study.

2004

In the present work we have investigated levels of stress-70 proteins in the gills of mussel Mytilus galloprovincialis collected seasonally from subtidal rocky shores at 6 different sites of the Rovinj coastal area (Northern Adriatic, Croatia). 1-D analysis (SDS-PAGE) using monoclonal mouse antibodies anti-HSP70 detected two bands of stress-70 proteins, 70 and 72 kDa constitutively present during the year. 2-D analysis (IEF+SDS-PAGE) proved that the antibodies used detected HSP70 (pI 5.7–5.9) and HSP72 (pI 5.5–5.6). The quantification of stress-70 proteins was possible using 200 ng of external HSP70 protein standard included on every blot. Maximal levels of HSP72 and HSP70 were observed in …

Gillanimal structuresImmunoblottingZoologyEnvironmental pollutionAcclimatizationMediterranean seaMediterranean SeaAnimalsElectrophoresis Gel Two-DimensionalHSP70 Heat-Shock ProteinsMolluscalcsh:Environmental sciencesGeneral Environmental Sciencelcsh:GE1-350Analysis of VariancebiologyEcologyfungiTemperatureHeat shock proteins; Mytilus galloprovincialis; Stress-70 proteins; HSP70; HSP72; Environmental pollutionMusselbiology.organism_classificationBivalviaMytilusBivalviaElectrophoresis Polyacrylamide GelSeasonsEnvironmental PollutionBiomarkersDensitometryEnvironmental MonitoringEnvironment international
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Zebrafish Reveals Different and Conserved Features of Vertebrate Neuroglobin Gene Structure, Expression Pattern, and Ligand Binding

2004

Neuroglobin has been identified as a respiratory protein that is primarily expressed in the mammalian nervous system. Here we present the first detailed analysis of neuroglobin from a non-mammalian vertebrate, the zebrafish Danio rerio. The zebrafish neuroglobin gene reveals a mammalian-type exon-intron pattern in the coding region (B12.2, E11.0, and G7.0), plus an additional 5'-non-coding exon. Similar to the mammalian neuroglobin, the zebrafish protein displays a hexacoordinate deoxy-binding scheme. Flash photolysis kinetics show the competitive binding on the millisecond timescale of external ligands and the distal histidine, resulting in an oxygen affinity of 1 torr. Western blotting, i…

GillsDNA Complementaryanimal structuresBlotting WesternDanioNeuroglobinNerve Tissue ProteinsIn situ hybridizationBiologyLigandsBinding CompetitiveBiochemistryRetinaDiffusionExonChloridesAnimalsCoding regionHistidineRNA MessengerCloning MolecularMolecular BiologyZebrafishConserved SequenceIn Situ HybridizationZebrafishMessenger RNAModels GeneticExonsOlfactory PathwaysCell Biologybiology.organism_classificationMolecular biologyIntronsRecombinant ProteinsGlobinsMitochondriaCell biologyOxygenRespiratory proteinKineticsGene Expression RegulationMicroscopy FluorescenceSpectrophotometryNeuroglobinJournal of Biological Chemistry
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The yeast osmosensitive mutant fps1Δ transformed by the cauliflower BobTIP1;1 aquaporin withstand a hypo-osmotic shock

2005

AbstractOsmoregulation plays an important role in cellular responses to osmotic stress in plants and in yeast. Aquaporins contribute to osmotic adjustment by facilitating transport of water or solutes across membranes. The tonoplastic water channel BobTIP1;1 (original name BobTIP26-1) genes are upregulated during dessication stress in cauliflower meristematic tissue. To investigate the physiological importance of BobTIP1;1, we expressed it in a Saccharomyces cerevisiae osmosensitive mutant fps1Δ. We showed that the defect in the yeast glycerol plasma membrane transporter is complemented by a plant cDNA encoding the aquaporin BobTIP1;1 which is localized in the vacuolar membrane of the compl…

GlycerolOsmotic stressOsmosisDNA ComplementarySaccharomyces cerevisiae ProteinsTime FactorsOsmotic shockSaccharomyces cerevisiaeMutantBlotting WesternGenes FungalBiophysicsAquaporinBrassicaSaccharomyces cerevisiaeOsmosisAquaporinsGenes PlantBiochemistryPolymerase Chain ReactionStructural BiologyGeneticsCloning MolecularFluorescent Antibody Technique Indirectγ-TIPMolecular BiologyPlant ProteinsbiologyAquaporinCell MembraneGenetic Complementation TestMembrane ProteinsWaterVacuolar membraneCell BiologyIntracellular Membranesbiology.organism_classificationYeastHypo-osmotic shockKineticsMembranePhenotypeBiochemistryGene Expression RegulationMutationVacuolesOsmoregulationElectrophoresis Polyacrylamide GelFEBS Letters
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Evidence for the formation of covalent bonds between macromolecules in the domain of the wall of Candida albicans mycelial cells

1989

An O-glycosylated mannoprotein, after its incorporation into the wall, showed an increase in its molecular weight, due at least to its association with N-glycosidic sugar chain(s). This was shown by rendering the material soluble after partial degradation of the wall structure. At present it is unknown whether this phenomenon is due to an additional transglycosylation process or whether the partial degradation of the wall solubilizes a supramolecular structure formed between the original O-glycosylated protein which becomes linked either directly or indirectly through a protein to the N-sugar chain(s).

GlycosylationMacromolecular SubstancesBlotting WesternBiophysicsSupramolecular chemistryPolysaccharideBiochemistryFungal ProteinsCell wallCell WallCandida albicansCandida albicansMolecular Biologychemistry.chemical_classificationGel electrophoresisMembrane Glycoproteinsbiologybeta-GlucosidaseAntibodies MonoclonalGlucan 13-beta-GlucosidaseCell Biologybiology.organism_classificationMolecular Weightcarbohydrates (lipids)ProteoglycanBiochemistrychemistryCovalent bondbiology.proteinBiophysicsProtein Processing Post-TranslationalMacromoleculeBiochemical and Biophysical Research Communications
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Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28

1990

Killer toxin K28, a 16 kd protein secreted by the wine yeast Saccharomyces cerevisiae strain 28, was reversibly bound by a column of Concanavalin A-Sepharose, confirming its glycoprotein nature. HPLC analysis of acid hydrolyzates of K28 toxin as well as Western-blots of beta-eliminated and/or endo H-treated killer toxin preparations probed with polyclonal alpha-toxin antibodies revealed that the carbohydrate moiety of K28 consists of D-mannose only, which is O-glycosidically linked via Ser/Thr residues to the protein part. The change in gel mobility of K28 after beta-elimination was caused by a decrease in molecular mass of about 1,800, corresponding to a carbohydrate moiety of 10 mannose r…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternSaccharomyces cerevisiaeMannoseSaccharomyces cerevisiaemedicine.disease_causeMicrobiologyChromatography Affinitychemistry.chemical_compoundmedicineMolecular BiologyAntibodies FungalChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular massToxinImmunochemistrySepharoseGeneral MedicineMycotoxinsbiology.organism_classificationKiller Factors YeastYeastchemistryBiochemistryPolyclonal antibodiesbiology.proteinGlycoproteinMannoseAntonie van Leeuwenhoek
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Maturation of barley cysteine endopeptidase expressed in Trichoderma reesei is distorted by incomplete processing

2002

Maturation of barley cysteine endopeptidase B (EPB) in Trichoderma reesei was studied with metabolic inhibitors, Western blotting, and immuno microscopy. The inactive 42-kDa recombinant EPB proprotein, first detected in apical cells, was sequentially processed in a time-dependent manner to a secreted polypeptide of 38.5 kDa, and thereafter, to polypeptides of 37.5, 35.5, and 32 kDa exhibiting enzyme activity both in the hyphae and culture medium. The sizes of the different forms of recombinant EPB were in accordance with molecular masses calculated from the deduced amino acid sequence, assuming cleavage at four putative Kex2p sites present in the 42-kDa proprotein. Both the liquid and the z…

GlycosylationglycosylationStereochemistryBlotting WesternMolecular Sequence DataImmunologyApplied Microbiology and BiotechnologyMicrobiologylaw.inventioncysteine proteinasemodified Golgi-like bodychemistry.chemical_compoundlawGeneticsAmino Acid SequenceProproteinMolecular BiologyPeptide sequenceTrichoderma reeseiGlycoproteinsTrichodermachemistry.chemical_classificationbiologyTunicamycinHordeumGeneral MedicineBrefeldin Abiology.organism_classificationKex2pRecombinant ProteinsEnzyme assayEnzyme ActivationMolecular WeightsecretionCysteine EndopeptidasesEnzymechemistryBiochemistryRecombinant DNAbiology.proteinProtein Processing Post-Translational
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Protective role of the complement regulatory protein human CD-55 in cardiac xenograft: a descriptive study and a revision of the literature.

2002

The limited and inadequate availability of organs from human donors has resulted in the utilisation of xenografts as an alternative tool. Nevertheless, hyperacute rejection (HAR) following xenograft determines the loss of the transplanted organ. The “primum movens” is the activation of the complement pathway mediated by the binding of natural xenogenic antibodies to the endothelium of the graft, followed by the lysis of the endothelial cells with subsequent oedema, thrombosis and necrosis of the transplanted organ. In this work we describe morphological and biomolecular observations of isolated human-decay accelerating factor (h-DAF, CD55) transgenic pig hearts, after perfusion for four hou…

Graft RejectionHistologyCD55 AntigensSwineEndothelial cells2734Blotting WesternTransplantation HeterologousComplementCell BiologyOrgan SizeImmunohistochemistryMicroscopy ElectronEndothelial cellMembrane glycoproteinCoronary CirculationGenetic engineering:6 - Ciencias aplicadas::61 - Medicina::611 - Anatomía [CDU]AnimalsHeart TransplantationHumansXenotransplantationAnatomyComplement; Endothelial cells; Genetic engineering; Membrane glycoproteins; Xenotransplantation; Anatomy; 2734; Histology; Cell Biology
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