Search results for "Limulus"

showing 7 items of 7 documents

Extraordinary stability of hemocyanins from L. polyphemus and E. californicum studied using infrared spectroscopy from 294 to 20 K

2016

International audience; Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. Here we give infrared spectroscopic evidence of a high stability towards exposure to sub-zero temperatures for hemocyanins from the arthropods Limulus polyphemus and Eurypelma californicum at different pH values. Small but distinct temperature induced changes of the secondary structure were observed, but a stable core of at least 40% α-helical structure is preserved as identified in the infrared spectra obtained between 294 and 20 K. The structural changes differ in detail somewhat for the two hemocyanins, with overall fewer changes observed in the case of E. californicum. No…

0301 basic medicineSpectrophotometry InfraredÉlectrochimieInfraredAnalytical chemistryGeneral Physics and AstronomyInfrared spectroscopySpectroscopieCold treatmentProtein Structure SecondaryArthropod Proteins03 medical and health scienceschemistry.chemical_compoundHorseshoe CrabsAnimalsPhysical and Theoretical ChemistryProtein secondary structurebiologySpectroélectrochimieSpidersbiology.organism_classificationTemperature inducedChimie Physique[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallography030104 developmental biologyMyoglobinchemistryPolyphemusLimulusHemocyaninsPhysical Chemistry Chemical Physics
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On the role of D-glucuronic acid in the aggregation of cells from the marine sponge Geodia cydonium.

1979

Abstract The aggregation receptor (AR) from the marine sponge GEODIA CYDONIUM was analyzed with respect to its monosaccharide composition. Three major sugars ( D -galactose, D -glucose and D -glucuronic acid) accounted for about 85 % of the total carbohydrate. Negative results with different lectins directed against D -galactosyl, N -acetyl- D -galactosaminyl and N -acetyl- D -glucosaminyl groups, respectively, showed that these sugars are serologically unreactive in AR. Positive serological reactions were obtained with CONCANAVALIN A and LIMULUS POLYPHEMUS agglutinin. AR also reacted strongly with the basic polymer poly- L -lysine. Reaggregation experiments performed on the basis of these …

Binding SitesbiologyImmunologyGalactoseGlucuronatesCarbohydratebiology.organism_classificationGlucuronic acidBinding CompetitiveGalactosidasesPoriferaSpongechemistry.chemical_compoundAgglutininGlucosechemistryBiochemistryConcanavalin ALimulusGalactosebiology.proteinAnimalsGeodiaDevelopmental BiologyCell AggregationDevelopmental and comparative immunology
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Endotoxins in ophthalmic viscosurgical devices.

2003

Purpose To measure the endotoxin concentration (EC) of 25 commercially available, hyaluronic acid- and hydroxypropylmethylcellulose-based (HPMC) ophthalmic viscosurgical devices (OVDs). Methods The in vitro Limulus amebocyte lysate (LAL) assay, which indicates the presence of endotoxins originating from gram-negative bacteria, was used to determine the EC. The procedure was performed according to the European Pharmacopoeia/USP. EC including duplicate determinations, negative controls, dilution series with control standard endotoxin, dilution series with sample extract and positive sample control. Results 16 OVDs (Amvisc®, Amvisc® Plus, Biolon®, Coatel®, Healon®, Healon® GV, Healon®5, HPMC O…

LactoseLimulus testOphthalmologic Surgical ProceduresMethylcelluloseSensitivity and Specificity03 medical and health sciences0302 clinical medicineGram-Negative BacteriaOxazinesHumansConcentration factorHyaluronic AcidLimulus TestEndophthalmitisChromatographyPositive sampleChemistryReproducibility of ResultsGeneral MedicineDilutionEndotoxinsOphthalmologyLimulus amebocyte lysateImmunology030221 ophthalmology & optometry030217 neurology & neurosurgery
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Human endothelial cell-based assay for endotoxin as sensitive as the conventional Limulus Amebocyte Lysate assay

2014

AbstractEndotoxin, also known as lipopolysaccharide (LPS) produced by bacteria can be present in any liquid or on any biomaterial even if the material is sterile. Endotoxin in mammals can cause fever, inflammation, cell and tissue damage and irreversible septic shock and death. In the body, endothelial cells making up the blood vasculature and endothelial cells in vitro rapidly react to minute amounts of endotoxin resulting in a rapid induction of the cell adhesion molecule E-selectin. In this study we have used immunofluorescent staining to evaluate the expression of E-selectin on human microvascular endothelial cells from the skin (HDMEC) and human umbilical vein endothelial cells (HUVEC)…

LipopolysaccharideCellBiophysicsLipopolysaccharideBioengineeringBiologyUmbilical veinEndothelialMicrobiologyBiomaterialschemistry.chemical_compoundEndotoxinLimit of DetectionHorseshoe CrabsmedicineAnimalsHumansCell adhesionCells CulturedCell adhesion moleculeIn vitroEndotoxinsEndothelial stem cellmedicine.anatomical_structurechemistryMechanics of MaterialsLimulus amebocyte lysateCeramics and CompositesLimulus amebocyte assayEndothelium VascularBiomaterials
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Limulus polyphemus Hemocyanin: 10 Å Cryo-EM Structure, Sequence Analysis, Molecular Modelling and Rigid-body Fitting Reveal the Interfaces Between th…

2007

Abstract The blue copper protein hemocyanin from the horseshoe crab Limulus polyphemus is among the largest respiratory proteins found in nature (3.5 MDa) and exhibits a highly cooperative oxygen binding. Its 48 subunits are arranged as eight hexamers (1×6mers) that form the native 8×6mer in a nested hierarchy of 2×6mers and 4×6mers. This quaternary structure is established by eight subunit types (termed I, IIA, II, IIIA, IIIB, IV, V, and VI), of which only type II has been sequenced. Crystal structures of the 1×6mer are available, but for the 8×6mer only a 40 A 3D reconstruction exists. Consequently, the structural parameters of the 8×6mer are not firmly established, and the molecular inte…

Models MolecularMolecular modelCryo-electron microscopyCopper proteinProtein subunitmedicine.medical_treatmentMolecular Sequence DataStructure-Activity RelationshipStructural BiologyHorseshoe CrabsmedicineAnimalsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCryoelectron MicroscopyHemocyaninbiology.organism_classificationProtein Structure TertiaryCrystallographyLimulusHemocyaninsProtein quaternary structureOxygen bindingJournal of Molecular Biology
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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Electron microscopy and biochemical characterization of a 350-kDa annular hemolymph protein from the keyhole limpet Megathura crenulata

1994

The isolation and biochemical characterization of an annular non-hemocyanin hemolymph protein from a marine gastropod, the Californian giant keyhole limpet (Megathura crenulata) is presented. By analytical ultracentrifugation, the protein has a sedimentation coefficient of 12S and molecular mass of approximately 350 kDa. The subunit mass, obtained by SDS/PAGE in the presence of -SH reagent and 8 M urea, is approximately 35 kDa, thereby indicating the presence of 10 subunits in the native molecule. By negative staining, the protein is revealed in one predominant image projection as a pentagonal approximately 8 nm ring-like structure with an approximately 2-nm stain-filled centre and, in anot…

biologyMolecular massProtein Conformationmedicine.medical_treatmentProtein subunitLimpetProteinsHemocyaninMegathura crenulatabiology.organism_classificationBiochemistryNegative stainMolecular WeightMicroscopy ElectronCrystallographyMolluscaHemolymphLimulusHemolymphmedicineBiophysicsAnimalsElectrophoresis Polyacrylamide GelUltracentrifugationEuropean Journal of Biochemistry
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