1998
Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis
Stone K, Deangelis R, LoPresti M, Jones J, Papov V, Williams K. Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Electrophoresis 1998, 19: 1046-1052. PMID: 9638951, DOI: 10.1002/elps.1150190620.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate-polyacrylamide gel electrophoresisQuadrupole ion trap mass spectrometerIon trap mass spectrometerDodecyl sulfate-polyacrylamide gel electrophoresisLow pmol levelSulfate-polyacrylamide gel electrophoresisIonization tandem mass spectrometryTrap mass spectrometerLiquid chromatography-electrospray ionization-tandem mass spectrometryLiquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysisMS/MS approachProtein identificationIonization tandem mass spectrometry analysisFmol levelFacile approachMass spectrometry analysisMass spectrometerEng et alMass spectrometryPmol levelLC-MS/MS approachTryptic digestMS approachSpectrometry analysisGel electrophoresis
1994
Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts.
Amrute S, Abdul-Manan Z, Pandey V, Williams K, Modak M. Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts. Biochemistry 1994, 33: 8282-91. PMID: 7518245, DOI: 10.1021/bi00193a015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleCell NucleusChromatographyChromatography, High Pressure LiquidCross-Linking ReagentsCyanogen BromideDNA, Single-StrandedHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataOligodeoxyribonucleotidesPeptide FragmentsRibonucleoproteinsRNASpectrometry, FluorescenceThymus GlandUltraviolet RaysConceptsHnRNP proteinsOccluded site sizeHeterogeneous nuclear ribonucleoproteinsNucleic acidsSingle-strand nucleic acidNH2-terminal sequencingEukaryotic RNATight tetramerSDS-polyacrylamide gel electrophoresisApparent molecular weightNuclear ribonucleoproteinNuclear extractsLimited proteolysisMass spectrometric analysisRNAProteinPhenylalanine 19Calf thymusGel electrophoresisAdditional ionic interactionsTerminal deoxynucleotidyl transferaseSite sizeAB formMajor siteCell disruption
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
1989
Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles
Merrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.Peer-Reviewed Original ResearchConceptsInsert sequenceHeterogeneous nuclear ribonucleoprotein particleSingle transcription unitAlternative splicing mechanismNuclear ribonucleoprotein particleAmino acid sequencingResidue insertHnRNP proteinsTranscription unitTryptic peptide mappingSplicing mechanismPrimary structure differencesC2 proteinSDS-polyacrylamide gel electrophoresisNuclear ribonucleoproteinProtein C1Ribonucleoprotein particleUntranslated regionPrimary structurePolyacrylamide gel electrophoresisAmino acidsPeptide mappingGel electrophoresisMolecular weight differencesProtein
1977
Purification and some properties of Escherichia coli tRNA nucleotidyltransferase.
Schofield P, Williams K. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. Journal Of Biological Chemistry 1977, 252: 5584-5588. PMID: 328503, DOI: 10.1016/s0021-9258(19)63390-9.Peer-Reviewed Original ResearchConceptsTransition metal chelating agentsMetal chelating agentsSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisSulfate gel electrophoresisTurnover numberChelating agentOverall yieldMolecular weightPure enzymeIsoelectric pointKey stepIdentical isoelectric pointsSephadex chromatographyCrude extractPurificationAffinity columnGel electrophoresisEscherichia coli tRNA nucleotidyltransferaseSpecific activityAssay conditionsChromatographyEnzymeTRNA nucleotidyltransferaseOptimal assay conditions