Search results for " Western"

showing 10 items of 687 documents

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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Shallow ocean oxygen decline during the end-Triassic mass extinction

2022

The end-Triassic mass extinction (ETME) was associated with intensified deep-water anoxia in epicontinental seas and mid-depth waters, yet the absolute oxygenation state in the shallow ocean is uncharacterized. Here we report carbonate-associated iodine data from the peritidal Mount Sparagio section (Southern Italy) that documents the ETME (~ 200 Ma) in the western Tethys. We find a sharp drop in carbonate I/(Ca + Mg) ratios across the extinction horizon and persisting into the Early Jurassic. This records local dissolved oxygen and iodate decline in the near-surface ocean of low-latitude Tethys due to the development of depleted oxygen concentrations. Consequently, during the ETME even sha…

Global and Planetary ChangeShallow ocean deoxygenationEnd-Triassic mass extinctionEnd-Triassic mass extinction I/(Ca + Mg) Shallow ocean deoxygenation Western TethysOceanographyEnd-Triassic mass extinction; I/(Ca + Mg); Shallow ocean deoxygenation; Western TethysI/(Ca + Mg)Western TethysGlobal and Planetary Change
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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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Nickel(II) inhibits the repair of O 6 -methylguanine in mammalian cells

1999

Nickel compounds are widespread carcinogens, and although only weakly mutagenic, interfere with nucleotide excision repair and with the repair of oxidative DNA base modifications. In the present study we investigated the effect of nickel(II) on the induction and repair of O6-methylguanine and N7-methylguanine after treatment with N-methyl-N-nitrosourea (MNU). We applied Chinese hamster ovary cells stably transfected with human O6-methylguanine-DNA methyltransferase (MGMT) cDNA (CHO-AT), and compared the results with the MGMT-deficient parental cell line. As determined by high-performance liquid chromatography/electrochemical detection (HPLC/ECD), there was a slight but mostly not significan…

GuanineMethyltransferaseDNA RepairHealth Toxicology and MutagenesisBlotting WesternHamsterMutagenCHO CellsBiologyTransfectionToxicologymedicine.disease_causeO(6)-Methylguanine-DNA MethyltransferaseNickelCricetinaemedicineAnimalsHumansCytotoxicityChromatography High Pressure LiquidCarcinogenChinese hamster ovary cellMethylnitrosoureaGeneral MedicineTransfectionMolecular biologyFemaleNucleotide excision repairArchives of Toxicology
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Fine-mapping of the B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen

2002

In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a carrier. It was found after Western blot analysis that three monoclonal antibodies (MAbs) (2-11B1, 3-11C2, HB.OT10) recognized the linear preS2 sequence within the amino acid (aa) stretch 3-WNSTTFHQTLQDP-13. The importance of each aa residue of the epitope was proved by comparison of antibody binding to alanine-substituted peptides in both free-peptide and Pepscan variants.

HBsAgmedicine.drug_classBlotting WesternMolecular Sequence DataImmunologyMonoclonal antibodyEpitopeMiceViral Envelope ProteinsmedicineAnimalsImmunology and AllergyAmino Acid SequenceProtein PrecursorsPeptide sequenceHepatitis B Surface AntigensLinear epitopebiologyAntibodies MonoclonalMolecular biologyEpitope mappingPepscanbiology.proteinEpitopes B-LymphocyteAntibodyEpitope MappingJournal of Immunological Methods
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