2012
Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins
Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins. Journal Of The American Society For Mass Spectrometry 2012, 23: 1716-1728. PMID: 22847390, DOI: 10.1007/s13361-012-0437-4.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyMass spectrometryIonization mass spectrometric studyHigh-resolution mass spectrometryDiagnostic fragment ionsResolution mass spectrometryMass spectrometric characterizationMass spectrometric studyChain length variationReversed-phase high-performance liquid chromatographyMS/MS analysisLaser desorption ionizationMass spectrometric analysisLinear precursorsFragment ionsMacrocyclic ringFatty acid chainsPerformance liquid chromatographySpectrometric characterizationGlu replacementSpectrometric studyAcid moietyComplex mixturesDesorption ionizationFatty acid moieties
1990
[21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins
Stone K, Elliott J, Peterson G, McMurray W, Williams K. [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins. Methods In Enzymology 1990, 193: 389-412. PMID: 2074828, DOI: 10.1016/0076-6879(90)93429-o.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyReversed-phase high-performance liquid chromatographyReversed phase high performance liquid chromatographyLiquid chromatographyEnzymatic digestsHigh peak capacityMass spectrometric approachProtein chemistsSpectrometric approachMass spectrometryPeak capacityComplex mixturesMolecular weightChemical cleavageGradient timeCleavage productsChromatographyTryptic peptidesPeptidesDigestsChemistsSpectrometryFractionationProductsPrimary structure
1987
Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.
Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.Peer-Reviewed Original ResearchConceptsCross-linking reactionReversed-phase high-performance liquid chromatographyHigh-performance liquid chromatographyCross-linking sitesEscherichia coli DNA polymerase IPeptide lossKlenow fragmentChelate formLiquid chromatographyAmino acid analysisE. coli DNA Pol ISmall peptidesTryptic digestionSubstrate deoxynucleoside triphosphateHistidine residuesTryptic peptidesAmino acidsSingle peptideOptimal conditionsPeptide mappingDNA Pol IStaphylococcus aureus V8 protease digestionDNA polymerase IAcceptor sitesPeptides
1977
A Liquid Chromatographic-Fluorometric Method for the Analysis of Picogram Amounts of Tryptophan Metabolites in Cerebrospinal Fluid
Anderson G, Purdy W. A Liquid Chromatographic-Fluorometric Method for the Analysis of Picogram Amounts of Tryptophan Metabolites in Cerebrospinal Fluid. Analytical Letters 1977, 10: 493-499. DOI: 10.1080/00032717708079393.Peer-Reviewed Original ResearchCerebrospinal fluidTryptophan metabolitesUntreated cerebrospinal fluidHigh-performance liquid chromatographyReversed-phase high-performance liquid chromatography
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