Search results for "Quaternary"

showing 10 items of 411 documents

Biogeography of the Pleistocene pleniglacial malacofaunas in Europe. Stratigraphic and climatic implications

1990

Abstract As determined by Lozek, malacological associations are significant of a particular vegetal environment. In Quaternary sequences, different types of associations are recognized which can be assimilated to the present types of malacofaunas. There are associations of grass group, of forest group and of the ecotone of these two biogeographical entities. On the European scale, in Pleistocene sequences, the interglacial faunas indicate similarly the same differences as today, being of stratigraphic interest. On the contrary, pleniglacial faunas, which are mainly preserved in the loess belt, seemed not interesting for stratigraphy since they indicate more generalized and more homogeneous …

PleistocenePaleontologyBiozoneBiostratigraphyOceanographyPaleontologyInterglacialFaciesPaleoecologyQuaternaryEcology Evolution Behavior and SystematicsGeologyHoloceneEarth-Surface ProcessesPalaeogeography, Palaeoclimatology, Palaeoecology
researchProduct

Novel cationic copolymers of a polyasparthylhydrazide: synthesis and characterization.

2005

Alpha,beta-poly(asparthylhydrazide) (PAHy), a water soluble synthetic polymer, was functionalized by using EDCI chemistry with 3-(carboxypropyl)trimethyl-ammonium chloride (CPTACl) obtaining carboxypropyltrimethyl ammonium copolymers (PAHy-CPTA). Three PAHy-CPTA copolymers at increasing derivatization degrees (38%, 48%, 58%) were chosen for subsequent investigations. The capability of these copolymers to bind, neutralize, and protect DNA against degradation by DNase II was evalued by gel retardation assay and DNA degradation test at pH 5.5. Zeta potential measurements show that all studied polymers are able to neutralize the anionic charge of DNA at polymer/DNA weight ratio in the range of …

PolymersPharmaceutical ScienceElectrophoretic Mobility Shift AssayElectrolyteChloridechemistry.chemical_compoundElectrolytesCationsPolymer chemistrymedicineCopolymerZeta potentialDerivatizationchemistry.chemical_classificationHEPESEndodeoxyribonucleasesCationic polymerizationpolyplexesGeneral MedicinePolymerDNAQuaternary Ammonium CompoundsCarbodiimideschemistryPeptidesmedicine.drugDrug delivery
researchProduct

Polystyrene Sulfonate–Porphyrin Assemblies: Influence of Polyelectrolyte and Porphyrin Structure

2011

In this study, electrostatic self-assembly of different polystyrene sulfonates and a set of tetravalent cationic porphyrins is investigated. It is shown that association of linear polystyrene sulfonates of different molar masses yields finite size nanoscale assemblies that are stable in aqueous solution. Aggregates are compared to the ones of cylindrical brushes, revealing that both form assemblies in the 100 nm range with the charge ratio (molar ratio of porphyrin charges to polyelectrolyte charges) being determining, while the morphology of the resulting network-like assemblies is different for both polyelectrolyte architectures. For the smallest 8k polystyrene sulfonate, in addition, sto…

PorphyrinsLightStatic ElectricityMicroscopy Atomic ForcePorphyrin structurePolystyrene sulfonatechemistry.chemical_compoundScattering Small AnglePolymer chemistryMaterials ChemistryScattering RadiationPhysical and Theoretical ChemistryCationic polymerizationPorphyrinPolyelectrolyteNanostructuresSurfaces Coatings and FilmsQuaternary Ammonium CompoundsNeutron DiffractionZincchemistryPolystyrenesSpectrophotometry UltravioletSelf-assemblyPolystyreneCopperThe Journal of Physical Chemistry B
researchProduct

Biological activities of the LXRα and β agonist, 4β-hydroxycholesterol, and of its isomer, 4α-hydroxycholesterol, on oligodendrocytes: effects on cel…

2013

The biochemical and biological properties of 4β-hydroxycholesterol and of its isomer, 4α-hydroxycholesterol, are not well known. So, we determined the ability of 4α- and 4β-hydroxycholesterol to react with LXRα and LXRβ, and we characterized the activities of these oxysterols on oligodendrocytes which are myelin synthesizing cells. The effects of 4α- and 4β-hydroxycholesterol were studied on 158N murine oligodendrocytes to assess their activities on cell growth and viability, oxidative and inflammatory status. To this end different parameters were used: cell counting with trypan blue; identification of dead cells and cell cycle analysis with propidium iodide; evaluation of mitochondrial dep…

Programmed cell deathCell SurvivalBiologyBiochemistrychemistry.chemical_compoundMiceIsomerismpolycyclic compoundsmedicineAnimalsPropidium iodideProtein Structure QuaternaryCell ProliferationLiver X ReceptorsInflammationSuperoxideCell growthAcridine orangeDepolarizationGeneral MedicineOrphan Nuclear ReceptorsOligodendrocyteActinsHydroxycholesterolsCell biologyMitochondriaOligodendrogliamedicine.anatomical_structurechemistryCytokineslipids (amino acids peptides and proteins)Trypan blueProtein MultimerizationLysosomesReactive Oxygen SpeciesOxidation-ReductionBiochimie
researchProduct

Specific processing of tenascin-C by the metalloprotease meprinβ neutralizes its inhibition of cell spreading

2009

The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-terminal pep…

Proteasesanimal structuresColonRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataTenascinCleavage (embryo)Cell LineCrohn DiseaseCell AdhesionAnimalsHumansProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologyAlternative splicingTenascin CMetalloendopeptidasesTenascinMolecular biologyPeptide FragmentsExtracellular MatrixFibronectinsFibronectinAlternative SplicingProtein Subunitsembryonic structuresbiology.proteinProtein MultimerizationChickensMatrix Biology
researchProduct

The molecular heterogeneity of hemocyanin: Structural and functional properties of the 4×6-meric protein of Upogebia pusilla (Crustacea)

2006

The structural properties of the hemocyanin isolated from the Mediterranean mud shrimp, Upogebia pusilla (Decapoda: Thalassinidea), were investigated. Our intent was to make use of the U. pusilla case to perform a structural comparison between crustacean and chelicerate 4×6-meric hemocyanins. The thalassinidean hemocyanin appears similar in size but different in structural organization compared to the chelicerate 4×6-mer. Ultracentrifuge analyses on the purified protein revealed a sedimentation coefficient of 39S, typical of 4×6 hemocyanins. Electron micrographs are in agreement with a model in which four 2×6-meric building blocks are arranged in a tetrahedron-like quaternary structure and …

Protein Conformation030310 physiologymedicine.medical_treatmentAllosteric regulationHemocyaninDivalent03 medical and health sciencesOxygen bindingDecapodaCatalytic propertiesGeneticsmedicineQuaternary structureAnimals030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyDecapodaHemocyaninGeneral Medicinebiology.organism_classificationHemocyanin; Quaternary structure; Dissociation; Oxygen binding; Catalytic propertiesMolecular WeightOxygenSedimentation coefficientMicroscopy ElectronchemistryBiochemistryHemocyaninsChromatography GelProtein quaternary structureUltracentrifugeDissociationOxygen bindingProtein BindingGene
researchProduct

Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1

2006

AbstractCentrins are members of the family of Ca2+-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resemb…

Protein ConformationAmino Acid MotifsSequence HomologyPlasma protein bindingEF-handTroponin CMiceStructure-Activity RelationshipProtein structureCalcium-binding proteinConnecting ciliumCentrinAnimalsHumansPhotoreceptor CellsCiliaEF Hand MotifsProtein Structure QuaternaryChemistryEF handCiliumCalcium-Binding ProteinsTerminal Repeat SequencesCalcium-binding proteinSensory SystemsProtein Structure TertiaryCell biologyOphthalmologyCentrinCalciumTransducinsense organsX-ray structureProtein BindingVision Research
researchProduct

Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin

1996

Small-angle X-ray scattering (SAXS) curves have been recorded for the oxygenated and deoxygenated states of the 4 x 6-meric hemocyanin from the tarantula Eurypelma californicum. A comparison of the curves shows that the quaternary structures of the two states are different by three criteria, which all indicate that the hemocyanin is less compact in the oxygenated compared to the deoxygenated form: (a) The radius of gyration is 8.65 +/- 0.05 nm for the deoxy- and 8.80 +/- 0.05 nm for the oxy-form. (b) The maximum particle dimension amounts to 25.0 +/- 0.5 nm for the deoxy- and to 27.0 +/- 0.5 nm for the oxy-form. (c) A dip in the intramolecular distance distribution function p(r) is more pro…

Protein Conformationmedicine.medical_treatmentBiophysicsElectronBiochemistrylaw.inventionX-Ray DiffractionStructural BiologylawGeneticsmedicineAnimalsMolecular BiologyChemistrySmall-angle X-ray scatteringScatteringSpidersHemocyaninCell BiologyModels StructuralMicroscopy ElectronCrystallographyIntramolecular forceHemocyaninsRadius of gyrationProtein quaternary structureElectron microscopeOxidation-ReductionFEBS Letters
researchProduct

Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin

2004

Hemocyanin sequences allineament shows the presence of highly invariant regions especially in the active site and in the tight intersubunits interaction sites. Comparing the aminoacids in contact regions between monomers is possible to interpret the stability of hexamers.

Protein Conformationmedicine.medical_treatmentGeneral Physics and AstronomyBiologyPenaeus monodon03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePenaeidaeStructural BiologymedicineAnimalsGeneral Materials Science030304 developmental biology0303 health sciencesEcologyActive siteHemocyaninCell Biologybiology.organism_classificationOxygenMonomerchemistryHemocyaninsBiophysicsbiology.proteinProtein quaternary structureConformational stability030217 neurology & neurosurgeryOxygen binding
researchProduct

Molecular mass of macromolecules and subunits and the quaternary structure of hemoglobin from the microcrustacean Daphnia magna

2006

The molecular masses of macromolecules and subunits of the extracellular hemoglobin from the fresh-water crustacean Daphnia magna were determined by analytical ultracentrifugation, multiangle laser light scattering and electrospray ionization mass spectrometry. The hemoglobins from hypoxia-incubated, hemoglobin-rich and normoxia-incubated, hemoglobin-poor Daphnia magna were analyzed separately. The sedimentation coefficient of the macromolecule was 17.4 +/- 0.1 S, and its molecular mass was 583 kDa (hemoglobin-rich animals) determined by AUC and 590.4 +/- 11.1 kDa (hemoglobin-rich animals) and 597.5 +/- 49 kDa (hemoglobin-poor animals), respectively, determined by multiangle laser light sca…

Protein DenaturationChromatography GasGlycosylationLightMacromolecular SubstancesProtein ConformationElectrospray ionizationProtein subunitDaphnia magnaMultiangle light scatteringBiologyBiochemistryHemoglobinsImaging Three-DimensionalAnimalsScattering RadiationProtein Structure QuaternaryMolecular BiologyChromatography High Pressure LiquidChromatographyMolecular massLasersfungiCell BiologyHemoglobin Subunitsbiology.organism_classificationMolecular WeightProtein SubunitsDaphniaFemaleProtein quaternary structureHemoglobinFEBS Journal
researchProduct