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dc.creatorMarco Arnulfo Mata Gómez
dc.date2012
dc.date.accessioned2018-10-18T21:51:12Z
dc.date.available2018-10-18T21:51:12Z
dc.identifier.issn19326203
dc.identifier.doi10.1371/journal.pone.0031438
dc.identifier.urihttp://hdl.handle.net/11285/630529
dc.descriptionBackground: The identification of proteins by mass spectrometry is a standard method in biopharmaceutical quality control and biochemical research. Prior to identification by mass spectrometry, proteins are usually pre-separated by electrophoresis. However, current protein staining and de-staining protocols are tedious and time consuming, and therefore prolong the sample preparation time for mass spectrometry. Methodology and Principal Findings: We developed a 1-minute covalent pre-gel staining protocol for proteins, which does not require de-staining before the mass spectrometry analysis. We investigated the electrophoretic properties of derivatized proteins and peptides and studied their behavior in mass spectrometry. Further, we elucidated the preferred reaction of proteins with Uniblue A and demonstrate the integration of the peptide derivatization into typical informatics tools. Conclusions and Significance: The Uniblue A staining method drastically speeds up the sample preparation for the mass spectrometry based identification of proteins. The application of this chemo-proteomic strategy will be advantageous for routine quality control of proteins and for time-critical tasks in protein analysis. © 2012 Mata-Gómez et al.
dc.languageeng
dc.relationhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84857160431&doi=10.1371%2fjournal.pone.0031438&partnerID=40&md5=2b06c232fe74e0fff017333066f541f6
dc.relationInvestigadores
dc.relationEstudiantes
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.sourcePLoS ONE
dc.subjectdye
dc.subjectunclassified drug
dc.subjectuniblue A
dc.subjectamino acid
dc.subjectanazolene sodium
dc.subjectanthraquinone derivative
dc.subjectEscherichia coli protein
dc.subjectfuchsine
dc.subjectpeptide
dc.subjectprotein
dc.subjectsulfonic acid derivative
dc.subjectaccuracy
dc.subjectarticle
dc.subjectchemical structure
dc.subjectcontrolled study
dc.subjectcovalent bond
dc.subjectderivatization
dc.subjectintermethod comparison
dc.subjectliquid chromatography
dc.subjectnucleophilicity
dc.subjectprediction
dc.subjectprocess development
dc.subjectprocess optimization
dc.subjectprotein analysis
dc.subjectprotein electrophoresis
dc.subjectprotein modification
dc.subjectproteomics
dc.subjectsensitivity and specificity
dc.subjectstaining
dc.subjecttandem mass spectrometry
dc.subjecttwo dimensional gel electrophoresis
dc.subjectvalidation process
dc.subjectamino acid sequence
dc.subjectbiology
dc.subjectchemistry
dc.subjectEscherichia coli
dc.subjectgel
dc.subjectmass spectrometry
dc.subjectmetabolism
dc.subjectmethodology
dc.subjectmolecular genetics
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectprotein database
dc.subjectstaining
dc.subjectstandard
dc.subjectAmino Acid Sequence
dc.subjectAmino Acids
dc.subjectAnthraquinones
dc.subjectChromatography, Liquid
dc.subjectComputational Biology
dc.subjectDatabases, Protein
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectGels
dc.subjectMass Spectrometry
dc.subjectMolecular Sequence Data
dc.subjectPeptides
dc.subjectProteins
dc.subjectReference Standards
dc.subjectRosaniline Dyes
dc.subjectStaining and Labeling
dc.subjectSulfonic Acids
dc.subject.classification7 INGENIERÍA Y TECNOLOGÍA
dc.titleAccelerated identification of proteins by mass spectrometry by employing covalent pre-gel staining with Uniblue A
dc.typeArtículo
dc.identifier.volume7
dc.identifier.issue2
refterms.dateFOA2018-10-18T21:51:12Z


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