Search results for "liquid"

showing 10 items of 4351 documents

Enhancing Sensitivity of Microflow-Based Bottom-Up Proteomics through Postcolumn Solvent Addition.

2019

The introduction of more sensitive mass spectrometers allows researchers to adapt front-end liquid chromatography (LC) to individual needs for the analysis of complex proteomes. Where absolute sensitivity is not paramount, it is advantageous to switch from a highly sensitive nanoflow-LC setup, the de facto standard platform in mass-spectrometry (MS)-based discovery proteomics, to a more robust, high-throughput-compatible microflow or conventional-flow setup. To enhance the microflow-LC-MS electrospray process of complex proteomic samples, we tested the effects of different solvents, including 2-propanol, methanol, and acetonitrile, pure or as mixture with dimethyl sulfoxide, which were adde…

ProteomicsElectrospraySpectrometry Mass Electrospray IonizationChromatographyChemistryDimethyl sulfoxideElectrospray ionization010401 analytical chemistry010402 general chemistryMass spectrometry01 natural sciences0104 chemical sciencesAnalytical ChemistrySolventchemistry.chemical_compoundSolventsHumansNanotechnologyDimethyl SulfoxideBottom-up proteomicsMethanolAcetonitrilePeptidesChromatography High Pressure LiquidHeLa CellsAnalytical chemistry
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Proteomics evaluation of enniatins acute toxicity in rat liver

2021

Abstract Enniatins (ENs) are emerging mycotoxins produced by Fusarium fungi which are cytotoxic also at low concentrations due to its ionophoric properties. The aim of this study was to evaluate the hepatic toxicity of ENs exposure at different concentrations in Wistar rats through a proteomic approach. Animals were intoxicated by oral gavage with medium (EN A 256, ENA1 353, ENB 540, ENB1 296 μg/mL) and high concentrations (ENA 513, ENA1 706, ENB 1021, ENB1 593 μg/mL) of an ENs mixture and sacrificed after 8 h. Protein extraction was performed using powdered liver. Peptides were analyzed using a liquid chromatography coupled with a quadrupole time-of-flight mass spectrometer. Proteins were …

ProteomicsFusariumToxicologyProteomicsmedicine.disease_cause03 medical and health sciences0404 agricultural biotechnologyTandem Mass SpectrometryIn vivoDepsipeptidesIn vivoProtein purificationmedicineAnimalsRats Wistar030304 developmental biology0303 health sciencesbiologyChemistry04 agricultural and veterinary sciencesGeneral MedicineMetabolismMycotoxinsbiology.organism_classification040401 food scienceAcute toxicityRatsLiverBiochemistryOxidative stressElectron transport chainFemaleNAD+ kinaseBiomarkersOxidative stressChromatography LiquidFood ScienceFood and Chemical Toxicology
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Nanoparticle Size Is a Critical Physicochemical Determinant of the Human Blood Plasma Corona: A Comprehensive Quantitative Proteomic Analysis

2011

In biological fluids, proteins associate with nanoparticles, leading to a protein "corona" defining the biological identity of the particle. However, a comprehensive knowledge of particle-guided protein fingerprints and their dependence on nanomaterial properties is incomplete. We studied the long-lived ("hard") blood plasma derived corona on monodispersed amorphous silica nanoparticles differing in size (20, 30, and 100 nm). Employing label-free liquid chromatography mass spectrometry, one- and two-dimensional gel electrophoresis, and immunoblotting the composition of the protein corona was analyzed not only qualitatively but also quantitatively. Detected proteins were bioinformatically cl…

ProteomicsGel electrophoresisChromatographyChemistryGeneral EngineeringGeneral Physics and AstronomyNanoparticleProtein CoronaMass spectrometryProteomicsMass SpectrometryPlasmaCorona (optical phenomenon)Liquid chromatography–mass spectrometryHumansNanoparticlesGeneral Materials ScienceParticle sizeParticle SizeBiologieACS Nano
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Unraveling the Composition of Insecticidal Crystal Proteins in Bacillus thuringiensis: a Proteomics Approach.

2020

ABSTRACT Bacillus thuringiensis (Bt) is the most widely used active ingredient for biological insecticides. The composition of δ-endotoxins (Cry and Cyt proteins) in the parasporal crystal determines the toxicity profile of each Bt strain. However, a reliable method for their identification and quantification has not been available, due to the high sequence identity of the genes that encode the δ-endotoxins and the toxins themselves. Here, we have developed an accurate and reproducible mass spectrometry-based method (liquid chromatography-tandem mass spectrometry-multiple reaction monitoring [LC-MS/MS-MRM]) using isotopically labeled proteotypic peptides for each protein in a particular mix…

ProteomicsInsecticidesProteomeQuantitative proteomicsBacillus thuringiensisProteomics01 natural sciencesApplied Microbiology and Biotechnology03 medical and health sciencesBiosafetyHemolysin ProteinsBacterial ProteinsTandem Mass SpectrometryBacillus thuringiensisInvertebrate Microbiology030304 developmental biologyPhytosanitary certificationActive ingredient0303 health sciencesChromatographyEcologybiologyBacillus thuringiensis ToxinsChemistry010401 analytical chemistrybiology.organism_classification0104 chemical sciencesEndotoxinsComposition (visual arts)FermentationFood ScienceBiotechnologyChromatography LiquidApplied and environmental microbiology
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Label-free profiling of skeletal muscle using high-definition mass spectrometry

2014

We report automated and time efficient (2 h per sample) profiling of muscle using ultra-performance liquid chromatography (LC) coupled directly with high-definition mass spectrometry (HDMSE). Soluble proteins extracted from rat gastrocnemius (n=10) were digested with trypsin and analysed in duplicate using a 90 min RPLC gradient. Protein identification and label-free quantitation were performed from HDMSE spectra analysed using TransOmics Informatics for Proteomics software. In total 1,514 proteins were identified. Of these, 811 had at least 3 unique peptides and were subsequently used to assess the dynamic range and precision of LC-HDMSE label-free profiling. Proteins analysed by LC-HDMSE …

ProteomicsMuscle Proteinsta3111ProteomicsMass spectrometryBiochemistryArticleMass Spectrometryion mobilityLiquid chromatography–mass spectrometryanimal proteomicsdata-independent acquisitionmedicineAnimalsData-independent acquisitionMuscle Skeletalta315Molecular Biologychemistry.chemical_classificationChromatographyta1184Skeletal muscleTricarboxylic acidTrypsinRatsLC-MSEnzymemedicine.anatomical_structurechemistryBiochemistryChromatography Liquidmedicine.drugPROTEOMICS
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Plant protein phosphorylation monitored by capillary liquid chromatography–element mass spectrometry

2007

Abstract Many essential cellular functions such as growth rate, motility, and metabolic activity are linked to reversible protein phosphorylation, since they are controlled by signaling cascades based mainly on phosphorylation/dephosphorylation events. Quantification of global or site-specific protein phosphorylation is not straightforward with standard proteomic techniques. The coupling of capillary liquid chromatography (μLC) with ICP-MS (inductively coupled plasma-mass spectrometry) is a method which allows a quantitative screening of protein extracts for their phosphorus and sulfur content, and thus provides access to the protein phosphorylation degree. In extension of a recent pilot st…

ProteomicsPhosphataseArabidopsisProtozoan ProteinsBiophysicsChlamydomonas reinhardtiimacromolecular substancesBiologyProteomicsBiochemistryMass SpectrometryDephosphorylationMiceAnimalsProtein phosphorylationPhosphorylationMolecular BiologyCells CulturedPlant ProteinsChromatographyArabidopsis ProteinsPhosphorusCell BiologyPhosphoproteinsbiology.organism_classificationPeptide FragmentsBiochemistryPlant proteinPhosphoproteinPhosphorylationChlamydomonas reinhardtiiSulfurChromatography LiquidBiochemical and Biophysical Research Communications
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LC–MS Based Cleavage Site Profiling of the Proteases ADAM10 and ADAM17 Using Proteome-Derived Peptide Libraries

2014

A Disintegrin and Metalloproteinase 10 (ADAM10) and ADAM17 catalyze ectodomain shedding of a number of cell surface proteins important for embryonic development and tissue homeostasis. Changes in the expression levels or dysregulated proteolytic activity of ADAM10 and ADAM17 have been shown to play important roles in multiple diseases such as inflammation, cancer, and neurodegenerative disorders. Despite the well documented substrate repertoire of ADAM10 and ADAM17, little is known about their cleavage site specificity. We optimized Q-PICS (Quantitative Proteomics for the Identification of Cleavage Sites) to elucidate the cleavage site specificity of recombinant murine ADAM10 and ADAM17. Tw…

ProteomicsProteasesProteomeQuantitative proteomicsADAM17 ProteinBiologyCleavage (embryo)BiochemistryMass SpectrometryADAM10 ProteinMicePeptide LibraryAnimalsHumansADAM17 ProteinPeptide libraryTissue homeostasisMembrane ProteinsGeneral ChemistryPeptide FragmentsADAM ProteinsBiochemistryEctodomainProteomeAmyloid Precursor Protein SecretasesChromatography LiquidJournal of Proteome Research
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Surfing transcriptomic landscapes. A step beyond the annotation of chromosome 16 proteome

2013

All participating laboratories are members of ProteoRed-ISCIII.-- et al.

ProteomicsProteomeSequence analysisBioinformaticsBiologyMicrobiologíaENCODEProteomicsBiochemistryMass SpectrometryTranscriptome03 medical and health sciencesAnnotationChromosome 16RNA-Seq. ENCODEHuman proteome projectHumansHuman proteome projectTranscriptomics030304 developmental biologyGenetics0303 health sciencesSequence Analysis RNA030302 biochemistry & molecular biologyGeneral ChemistryChromosome 163. Good healthProteomeTranscriptomeChromosomes Human Pair 16Chromatography Liquid
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"Design and application of a data-independent precursor and product ion repository."

2012

The functional design and application of a data-independent LC-MS precursor and product ion repository for protein identification, quantification, and validation is conceptually described. The ion repository was constructed from the sequence search results of a broad range of discovery experiments investigating various tissue types of two closely related mammalian species. The relative high degree of similarity in protein complement, ion detection, and peptide and protein identification allows for the analysis of normalized precursor and product ion intensity values, as well as standardized retention times, creating a multidimensional/orthogonal queryable, qualitative, and quantitative spac…

ProteomicsRelational databaseTandem mass spectrometryMass SpectrometryPRI BIOS Applied Genomics & ProteomicsIonprotein identificationStructural BiologyLiquid chromatography–mass spectrometryspectral librarytandem mass-spectrometryInstrumentation (computer programming)large-scale proteomicsDatabases ProteinPeptide sequenceSpectroscopylc-msComplement (set theory)IonsChemistryProteinsReproducibility of Resultsacquisitionresolutionms/ms spectraCombinatorial chemistryquantificationIdentification (information)Database Management SystemsPeptidesBiological systemChromatography Liquidpeptide identificationJournal of the American Society for Mass Spectrometry
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Serum and antibodies of glaucoma patients lead to changes in the proteome, especially cell regulatory proteins, in retinal cells.

2012

PURPOSE: Previous studies show significantly specifically changed autoantibody reactions against retinal antigens in the serum of glaucoma and ocular hypertension (OHT) patients in comparison to healthy people. As pathogenesis of glaucoma still is unknown the aim of this study was to analyze if the serum and antibodies of glaucoma patients interact with neuroretinal cells. METHODS: R28 cells were incubated with serum of patients suffering from primary open angle glaucoma (POAG), normal tension glaucoma (NTG) or OHT, POAG serum after antibody removal and serum from healthy people for 48 h under a normal or an elevated pressure of 15000 Pa (112 mmHg). RGC5 cells were additionally incubated wi…

ProteomicsRetinal Ganglion CellsSerumProteomegenetic structuresOcular hypertensionGlaucomalcsh:MedicineAutoimmunityPathogenesischemistry.chemical_compoundMolecular Cell Biologylcsh:ScienceCellular Stress ResponsesMultidisciplinarySpectrometric Identification of ProteinsbiologyNeurodegenerative DiseasesBlood proteinsSignaling CascadesNeurologyMedicineRetinal DisordersElectrophoresis Polyacrylamide GelAntibodyGlaucoma Open-AngleRetinal NeuronsSignal TransductionResearch ArticleSpectrometry Mass Electrospray IonizationImmunologyImmunoglobulinsPeptide MappingAntibodiesStress Signaling CascadeCell LineAntigenmedicinePressureAnimalsHumansBiologylcsh:RAutoantibodyRetinalGlaucomamedicine.diseaseeye diseasesRatsOphthalmologychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinOcular HypertensionClinical Immunologylcsh:Qsense organsChromatography LiquidPLoS ONE
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