Search results for "Divalent"

showing 10 items of 102 documents

Naturally occurring hemolysins in the coelomic fluid of Holothuria polii delle chiaie (Echinodermata).

1979

Abstract The coelomic fluid of Holothuria polii D.Ch contains hemolytic activity against erythrocytes of several vertebrate species. The hemolytic potency depends upon calcium ion concentration and varies according to erythrocyte source and cell number in the reaction mixture. Absorption experiments with formalinized rabbit erythrocytes suggest that hemolytic activity is not specific. Its heat lability, water insolubility at low pH values, and sensitivity to proteolytic enzymes suggest that hemolytic activity resides in protein molecules. The activity, maximal in alkaline media, appears to depend up time and temperature.

ErythrocytesCations DivalentSea CucumbersImmunologyDose-Response Relationship Immunologicchemistry.chemical_elementCalciumHemolysisHemolysin ProteinsPotencyAnimalsbiologyLabilityProteolytic enzymesTemperatureHemolysinExudates and TransudatesHydrogen-Ion Concentrationbiology.organism_classificationKineticschemistryBiochemistryCoelomAbsorption (chemistry)HolothuriaDevelopmental BiologyEchinodermataDevelopmental and comparative immunology
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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Design of ordered bimetallic complexes, Part 2:Trans-1,2-cyclohexanediaminetetraacetate bimetallates

1987

Knowledge of the kinetic and thermodynamic behaviour of aqueous solutions containing two divalent cations andtrans-1,2-cyclohexanediaminetetraacetate has been used to design synthetic pathways to ordered bimetallic complexes

Inorganic Chemistrychemistry.chemical_classificationchemistry.chemical_compoundAqueous solutionchemistryComputational chemistryInorganic chemistryMaterials ChemistryMetals and AlloysBimetallic stripOrganometallic chemistryDivalentCatalysisTransition Metal Chemistry
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Heptacoordinated MnIIin oxalate-based bimetallic 2D magnets: synthesis and characterisation of [Mn(L)6][Mn(CH3OH)MIII(ox)3]2(MIII= Cr, Rh; ox = oxala…

2006

Oxalate-based magnets have been known with several different crystallographic structures, from 1D to 3D, but with all of them based in metal ions with octahedral coordination. In this article we report a new bidimensional oxalate-bridged bimetallic magnet where the divalent metal appears heptacoordinated, which has strong effects in the structure and properties of this materials.

Inorganic Chemistrychemistry.chemical_compoundCrystallographyMaterials scienceOctahedronchemistryMagnetMetal ions in aqueous solutionNanotechnologyBimetallic stripOxalateDivalent metalDalton Trans.
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Sorption of copper(II) ions in the biomass of alga Spirogyra sp.

2012

Abstract Sorption of copper ions by the alga Spirogyra sp. was investigated to determine the influence of experimental conditions and the methods of sample preparation on the process. The experiments were carried out both under the static and the dynamic conditions. Kinetics and equilibrium parameters of the sorption were evaluated. In addition, the influence was studied of the algae preparation methods on the conductivity of demineralized water in which the algae samples were immersed. The static experiments showed that the sorption of Cu2+ ions reached equilibrium in about 30 min, with approximately 90% of the ions adsorbed in the initial 15 min. The sorption capacity determined from the …

LangmuirCations DivalentInorganic chemistryBiophysicschemistry.chemical_elementFresh WaterConductivityAdsorptionAlgaeElectrochemistrySample preparationBiomassPhysical and Theoretical ChemistrybiologyElectric ConductivityTemperatureSorptionGeneral MedicineHydrogen-Ion ConcentrationSpirogyrabiology.organism_classificationCopperSolutionsKineticsBiodegradation EnvironmentalchemistryVolume (thermodynamics)Environmental chemistryThermodynamicsAdsorptionCopperWater Pollutants ChemicalBioelectrochemistry
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Understanding the Stabilization and Tunability of Divalent Europium 2.2.2B Cryptates

2021

Lanthanides such as europium with more accessible divalent states are useful for studying redox stability afforded by macrocyclic organic ligands. Substituted cryptands, such as 2.2.2B cryptand, that increase the oxidative stability of divalent europium also provide coordination environments that support synthetic alterations of Eu(II) cryptate complexes. Two single crystal structures were obtained containing nine-coordinate Eu(II) 2.2.2B cryptate complexes that differ by a single coordination site, the occupation of which is dictated by changes in reaction conditions. A crystal structure containing a [Eu(2.2.2B)Cl]+ complex is obtained from a methanol-THF solvent mixture, while a methanol-…

Lanthanidechemistry.chemical_classificationLigandCryptandchemistry.chemical_elementCrystal structureDivalentInorganic ChemistryCrystallographychemistryMoleculePhysical and Theoretical ChemistryEuropiumSingle crystalInorganic Chemistry
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Synthesis and coordination properties of an azamacrocyclic Zn(II) chemosensor containing pendent methylnaphthyl groups

2008

The synthesis of a polyazamacrocycle constituted by two diethylenetriamine bridges functionalized at their central nitrogen with naphth-2-ylmethyl units and interconnected through 2,6-dimethylpyridine spacers (L1) is reported. The protonation behaviour of the new macrocycle in water and in water-ethanol 70/30 v/v mixed solvent has been examined by means of pH-metric, UV-Vis and steady-state fluorescence techniques. The fluorescence emission is slightly quenched following the deprotonation of the central tertiary amines and more deeply quenched upon deprotonation of the secondary amino groups. pH-Metric titrations show that in water-ethanol 70/30 v/v L1 forms stable mononuclear complexes wit…

Macrocyclic CompoundsMetal ions in aqueous solutionProtonationNaphthalenesLigandsPhotochemistryChemistry Techniques AnalyticalFluorescenceDivalentInorganic Chemistrychemistry.chemical_compoundDeprotonationOrganometallic CompoundsTransition ElementsQualitative inorganic analysischemistry.chemical_classificationAza CompoundsTemperatureHydrogen-Ion ConcentrationPhotochemical ProcessesFluorescenceZincCrystallographychemistryDiethylenetriamineTitrationProtonsDalton Transactions
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Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100

1979

1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5…

Macromolecular SubstancesSize-exclusion chromatographyRhodospirillum rubrumBiochemistryPolyethylene GlycolsSubstrate SpecificityDivalentchemistry.chemical_compoundMoietyAmino AcidsSodium dodecyl sulfateAdenosine Triphosphataseschemistry.chemical_classificationChromatographyMolecular massbiologyChemistryIsoelectric focusingRhodospirillum rubrumBacterial Chromatophoresbiology.organism_classificationMolecular WeightKineticsOxidative Phosphorylation Coupling FactorsTriton X-100OligomycinsEuropean Journal of Biochemistry
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Purification of a glucose-binding protein from rat liver nuclei. Evidence for a role in targeting of nuclear mRNP to nuclear pore complex.

1992

A nuclear carbohydrate-binding protein with a molecular mass of 67 kDa (CBP67), which is specific for glucose residues, was purified to essential homogeneity from rat liver nuclear extracts. This protein could also be isolated from nuclear ribonucleoprotein (RNP) complexes by extraction in the presence of 0.6 M or 2 M NaCl, but it was absent in polysomal RNP complex. The binding of the purified protein, which has an isoelectric point of 7.3, to glucose-containing glycoconjugates depends on the presence of Ca2+ and Mg2+. Using closed nuclear envelope vesicles as a system to study nuclear transport of RNA, it was shown that both entrapped polysomal mRNA and nuclear RNA precursors are readily …

MaleMonosaccharide Transport ProteinsCations DivalentBiologyBiochemistryAnimalsHumansMagnesiumRNA MessengerNuclear proteinNuclear poreCell NucleusBinding proteinNuclear cap-binding protein complexBiological TransportRats Inbred StrainsRatsMessenger RNPGlucose bindingMolecular WeightBiochemistryLiverRibonucleoproteinsCalciumElectrophoresis Polyacrylamide GelNucleoporinNuclear transportIsoelectric FocusingHeLa CellsEuropean journal of biochemistry
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Different deoxyribonucleases in human lymphocytes

1974

Abstract The distribution pattern of deoxyribonuclease activities in human lymphocytes has been examined by micro-disc-electrophoresis. Four groups of deoxyribonuclease activities, differing in their electrophoretic mobility, in the nature of their optimal substrate and in their optimal incubation conditions, are characterized. There are two alkaline DNase-activities. One corresponds to DNase I (EC 3.1.4.5), the other having pH optimum of about pH 9.0, prefers denatured DNA as substrate and is not dependent on divalent cations. The fractions with an acid pH optimum can be subdivided into two groups, which differ in their activity towards native DNA, towards denatured DNA, in their activity …

Malechemistry.chemical_classificationDeoxyribonucleasesHot TemperatureSubstrate (chemistry)DeoxyribonucleaseHydrogen-Ion ConcentrationIn Vitro TechniquesBiologyDivalentElectrophoresischemistry.chemical_compoundchemistryBiochemistryGeneticsHumansElectrophoresis Polyacrylamide GelLymphocytesDeoxyribonuclease IDeoxyribonucleasesIncubationDNANucleic Acids Research
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