2009
Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins
Stone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins. Springer Protocols Handbooks 2009, 941-950. DOI: 10.1007/978-1-59745-198-7_102.Peer-Reviewed Original ResearchLaser desorption mass spectrometrySites of chemicalHigh pressureUltra-high pressureRelative elution positionsBroad peakDesorption mass spectrometryPowerful techniquePhase resultsMobile phase resultsReversed-phase HPLCEnzymatic digestsLC systemRelevant parametersMatrix-assisted laser desorption mass spectrometryMass spectrometric approachReversed-phase HPLC separationReversephase HPLCTotal hydrophobicitySpectrometric approachAqueous mixturesMass spectrometryVolatile solventsResolutionHPLC separation
2002
Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins
Stone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins. 2002, 0: 533-540. DOI: 10.1385/1-59259-169-8:533.Peer-Reviewed Original ResearchReversed-phase HPLCEnzymatic digestsLaser desorption mass spectrometrySites of chemicalMatrix-assisted laser desorption mass spectrometryRelative elution positionsDesorption mass spectrometryMobile phase resultsReversed-phase HPLC separationTotal hydrophobicityAqueous mixturesMass spectrometryVolatile solventsReversephase HPLCHPLC separationLarge peptidesParticular separationComplex mixturesExcellent reproducibilitySlow kineticsEdman sequencingRetention coefficientTight bindingHydrophobic amino acidsHPLC
1996
Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels
Stone K, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels. Springer Protocols Handbooks 1996, 415-425. DOI: 10.1007/978-1-60327-259-9_71.Peer-Reviewed Original ResearchGel digestion procedurePolyacrylamide gel matrixPolyacrylamide gelsFree NH2 terminusPeptide fractionationCleavage procedurePonceau SGel matrixFinal purificationReversed-phase HPLCSDS-polyacrylamide gelsChemical cleavageDigestion procedureCoomassie blueProteolytic digestionSitu digestionEnzymatic digestionGelEdman degradationNitrocellulose membraneMost eukaryotic proteinsSDS-PAGEPVDFSolutionDigestionReverse-Phase HPLC Separation of Enzymatic Digests of Proteins
Stone K, Williams K. Reverse-Phase HPLC Separation of Enzymatic Digests of Proteins. Springer Protocols Handbooks 1996, 427-434. DOI: 10.1007/978-1-60327-259-9_72.Peer-Reviewed Original ResearchReversed-phase HPLCEnzymatic digestsLaser desorption mass spectrometrySites of chemicalMatrix-assisted laser desorption mass spectrometryRelative elution positionsDesorption mass spectrometryMobile phase resultsReversed-phase HPLC separationTotal hydrophobicityAqueous mixturesMass spectrometryVolatile solventsHPLC separationLarge peptidesComplex mixturesParticular separationExcellent reproducibilitySlow kineticsEdman sequencingRetention coefficientTight bindingHydrophobic amino acidsHPLCRelative insolubility
1995
Digestion of Proteins in Gels for Sequence Analysis
Stone K, Williams K. Digestion of Proteins in Gels for Sequence Analysis. Current Protocols In Protein Science 1995, 00: 11.3.1-11.3.13. DOI: 10.1002/0471140864.ps1103s00.Peer-Reviewed Original ResearchProtein samplesSDS-PAGEDigestion of proteinsSDS-polyacrylamide gelsAbsence of detergentCDNA cloningAmino terminusPartial sequencesSequencing studiesSequence analysisInternal sequencingInhibits trypsinAmino acid analysisAmount of proteinProteinAlternate protocolGel slicesAcid analysisEnzymatic cleavageReversed-phase HPLCSubsequent washing stepsResidual SDSPmol amountsCloningTerminus
1992
Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins
Stone K, LoPresti M, Williams K, Mcnulty D, Crawford J, DeAngelis R. Elution and Internal Amino Acid Sequencing of PVDF-Blotted Proteins. 1992, 23-34. DOI: 10.1016/b978-0-12-058756-8.50008-0.Peer-Reviewed Original ResearchPVDF membranePolyacrylamide gel electrophoresisPolyvinylidene difluoride membraneTryptic digestMolecular weightReversed-phase HPLCSDS-polyacrylamide gel electrophoresisHigh yieldsTotal purificationDifluoride membraneEnzymatic cleavageTryptic peptidesPhase HPLCCyanogen bromide peptidesCyanogen bromide cleavageCleavageInternal amino acid sequencingGel electrophoresisPeptidesAmino acid sequencingMembraneElutionPurification
1987
Use of HPLC Comparative Peptide Mapping in Structure/Function Studies
Williams K, Stone K, Fritz M, Merrill B, Konigsberg W, Pandolfo M, Valentini O, Riva S, Reddigari S, Patel G, Chase J. Use of HPLC Comparative Peptide Mapping in Structure/Function Studies. 1987, 45-52. DOI: 10.1007/978-1-4613-1787-6_5.Peer-Reviewed Original ResearchComparative peptide mappingPeptide mappingActive site peptideGroup-specific reagentsStructure/function studiesGas-phase sequencingProtein structureChemical modificationActive siteCovalent crosslinkingEnzymatic digestsReversed-phase HPLCSite peptideRetention timeSpecific reagentsPhase sequencingHPLCStructureBaseline artifactsIndividual amino acidsLigandsSpecific applicationsPeptidesReagentsAmino acids