2019
Characterization of buffalo native pregnancy-associated glycoprotein: mass spectrometry-based glycan composition analysis, sugar-binding characteristics and proteolytic activity assay
Lotfan M, Choudhary S, Yadav M, Tripathi I, Bhan S, Bathla S, Rawat P, Kumar S, Mohanty T, Kaushik J, Mohanty A. Characterization of buffalo native pregnancy-associated glycoprotein: mass spectrometry-based glycan composition analysis, sugar-binding characteristics and proteolytic activity assay. Journal Of Proteins And Proteomics 2019, 10: 23-32. DOI: 10.1007/s42485-018-00003-5.Peer-Reviewed Original ResearchPregnancy-associated glycoproteinsSugar-binding characteristicsProteolytic activityHigh-resolution mass spectrometryN-glycan structuresO-glycan structuresProteolytic activity assaysGlycosylated secretory proteinsPresence of glycosylationInhibitor pepstatin AGlycan structuresSecretory proteinsGlycan analysisActive peptidaseEmission maximumAffinity chromatographyMass spectrometryFluorescence quenching assayFoetal cotyledonsPepstatin ASDS-PAGEAnion exchangeOuter epithelial cell layerActivity assayPH range
2017
Constitutive and activation-dependent phosphorylation of lymphocyte phosphatase-associated phosphoprotein (LPAP)
Kruglova N, Meshkova T, Kopylov A, Mazurov D, Filatov A. Constitutive and activation-dependent phosphorylation of lymphocyte phosphatase-associated phosphoprotein (LPAP). PLOS ONE 2017, 12: e0182468. PMID: 28827793, PMCID: PMC5565103, DOI: 10.1371/journal.pone.0182468.Peer-Reviewed Original ResearchConceptsLymphocyte phosphatase-associated phosphoproteinPhorbol 12-myristate 13-acetateSer-99Ser-163Ser-153Ser-172Site-directed mutagenesisActivation-dependent phosphorylationActivation of T cellsPhospho-specific antibodiesLPAP phosphorylationFunction of LPAPPhosphorylation eventsPhosphorylation sitesSDS-PAGE techniqueMass spectrometry analysisT cell signalingCo-receptors CD4Kinase LckCo-regulationPhosphatase CD45Biological roleT cellsPhosphorylationSDS-PAGE
2014
SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells
Stoops EH, Farr GA, Hull M, Caplan MJ. SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells. Methods In Molecular Biology 2014, 1174: 171-182. PMID: 24947381, DOI: 10.1007/978-1-4939-0944-5_11.Peer-Reviewed Original ResearchConceptsMembrane proteinsSNAP-tagTrans-Golgi networkPolarized epithelial cellsBasolateral membrane proteinsSNAP-tag systemEpithelial cellsFluorescence microscopic analysisBiochemical approachesPlasma membraneTrafficking routesSubcellular distributionProteinConfocal microscopySDS-PAGEMicroscopic analysisTagsCellsTraffickingTag systemMembranePool
2009
Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels
Stone K, Gulcicek E, Williams K. Enzymatic Digestion of Proteins in Solution and in SDS Polyacrylamide Gels. Springer Protocols Handbooks 2009, 905-917. DOI: 10.1007/978-1-59745-198-7_99.Peer-Reviewed Original ResearchProtein of interestSDS-polyacrylamide gelsMass spectrometryGel digestion procedureChemical sequencingLaser desorption ionization mass spectrometryDesorption ionization mass spectrometryElectrospray ionization sourceIonization mass spectrometryComplex biological mixturesMass spectral acquisitionProtein identification analysisTandem mass spectrometrySDS-PAGEMass spectrometric analysisPolyacrylamide gelsIonization sourceNumerous genomesBiological mixturesPeptide mass dataProtein databaseCleavage procedureMass spectrometerGel matrixLC system
2008
Heterozygous expression of myocilin glaucoma mutants increases secretion of the mutant forms and reduces extracellular processed myocilin.
Aroca-Aguilar JD, Sánchez-Sánchez F, Martínez-Redondo F, Coca-Prados M, Escribano J. Heterozygous expression of myocilin glaucoma mutants increases secretion of the mutant forms and reduces extracellular processed myocilin. Molecular Vision 2008, 14: 2097-108. PMID: 19023451, PMCID: PMC2585175.Peer-Reviewed Original ResearchConceptsWild-type myocilinWild-type proteinMyocilin mutantsMutant myocilinMutant formsProteolytic processingMissense mutant formsHEK 293T cellsMyocilin geneMutant proteinsSecretory pathwayUnidentified functionExtracellular proteinsMutantsEndoproteolytic processingRecombinant mutantsMyocilin secretionCellular fractionsHeterozygous expressionMyocilinProteinUnknown mechanismExtracellular amountSDS-PAGEHeterozygous state
2002
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. 2002, 0: 511-521. DOI: 10.1385/1-59259-169-8:511.Peer-Reviewed Original ResearchPolyacrylamide gel matrixFree NH2 terminusPeptide fractionationCleavage procedureGel matrixFinal purificationChemical cleavagePolyacrylamide gelsEdman degradationMost eukaryotic proteinsSDS-polyacrylamide gelsPVDFGelSpecific proteasesPurificationSDS-PAGECleavageNH2 terminusFractionationPartial amino acid sequenceDegradation
1999
The Catalytic Mechanism of EPSP Synthase Revisited †
Lewis J, Johnson K, Anderson K. The Catalytic Mechanism of EPSP Synthase Revisited †. Biochemistry 1999, 38: 7372-7379. PMID: 10353849, DOI: 10.1021/bi9830258.Peer-Reviewed Original ResearchMeSH Keywords3-Phosphoshikimate 1-CarboxyvinyltransferaseAlkyl and Aryl TransferasesAmino Acid SubstitutionBinding SitesCatalysisChromatography, High Pressure LiquidEscherichia coliFreezingKineticsMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhosphoenolpyruvateProtonsSubstrate SpecificityConceptsEPSP synthaseEnzyme intermediateKinetic competenceSingle-turnover experimentsSubstrate to productSolid-state NMRSolid-state NMR studiesEnzyme assaysEnzyme reaction pathwaySDS-PAGECatalytic mechanismDegrees CSpeciesEnzymeIntermediate speciesNMR studiesSide productsCharacterized reaction productsSample preparationDisappearance of substrateSynthaseReaction productsFormation of productsBreakdown productsReaction pathways
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-PAGEPVDFSolutionDigestion
1995
Associations of the Epithelial Mucin, PAS-1, with Yield, Health, and Reproductive Traits in Holstein Dairy Cows
Hens JR, Rogers GW, Huott ML, Patton S. Associations of the Epithelial Mucin, PAS-1, with Yield, Health, and Reproductive Traits in Holstein Dairy Cows. Journal Of Dairy Science 1995, 78: 2473-2480. PMID: 8747338, DOI: 10.3168/jds.s0022-0302(95)76875-8.Peer-Reviewed Original ResearchDigestion 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
1994
Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ.
Brown E, Marquardt J, Lee J, Walsh C, Anderson K. Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ. Biochemistry 1994, 33: 10638-45. PMID: 8075064, DOI: 10.1021/bi00201a010.Peer-Reviewed Original ResearchConceptsUDP-N-acetylglucosamineUDP-GlcNAcAbsence of UDP-GlcNAcChemical quench analysisPresence of UDP-GlcNAcSingle-turnover conditionsBinding constantsPeptidoglycan biosynthesisSolution NMRC-2Enzyme nucleophilePeptide of molecular weightStoichiometric labelingConsistent with catalysisRemoval of small moleculesE. coliAdductsSmall moleculesMurZEnzyme adductNon-covalentlySDS-PAGEM ureaLabeled peptidesEnzymePurification of Human and Rat Kidney Aldose Reductase
Moeckel G, Hallbach J, Guder W. Purification of Human and Rat Kidney Aldose Reductase. Enzyme And Protein 1994, 48: 45-50. PMID: 7787970, DOI: 10.1159/000474968.Peer-Reviewed Original ResearchConceptsPurification of humanAldose reductaseRat kidney papillaRat kidney aldose reductaseSubstrate specificityHuman enzymeAffinity chromatographic procedureBlue SepharoseSDS-PAGESimilar molecular weightReductaseEnzymeMolecular weightSingle bandChromatographic procedureSorbitol formationKinetic constantsKidney papillaHuman kidneyHumansInner medulla
1993
Biological activity of recombinant human myelin basic protein
Oettinger H, Al-Sabbagh A, Jingwu Z, LaSalle J, Weiner H, Hafler D. Biological activity of recombinant human myelin basic protein. Journal Of Neuroimmunology 1993, 44: 157-162. PMID: 7685037, DOI: 10.1016/0165-5728(93)90037-y.Peer-Reviewed Original ResearchConceptsRecombinant human myelin basic proteinRecombinant protein bindsRecombinant MBPInducible expression vectorBasic proteinMyelin basic proteinRecombinant protein preparationsProtein bindsHuman myelin basic proteinRecombinant proteinsExpression vectorEscherichia coliProtein preparationsProteinNative MBPE. coliCation exchange chromatographySDS-PAGEBiological reagentsSimilar affinityHuman MBPColiBiological activitySimilar conformationsCell clones
1992
Dimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling
Engelman D, Adair B, Brünger A, Flanagan J, Lemmon M, Treutlein H, Zhang J. Dimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling. Jerusalem Symposia 1992, 25: 115-125. DOI: 10.1007/978-94-011-2718-9_11.Peer-Reviewed Original ResearchTransmembrane domainSingle transmembrane domainSite-specific mutagenesisGpA dimerTransmembrane helicesDeletion mutagenesisTransmembrane portionCarboxy terminusDimer interfaceHanded supercoilMutagenesisChimera formLipid bilayersGlycophorin AStaphylococcal nucleaseHuman erythrocyte sialoglycoproteinSDS-PAGEErythrocyte sialoglycoproteinDimerizationClose associationDomainDimersSupercoilsNucleaseTerminus
1989
ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus
Williams K, Hemmings H, LoPresti M, Greengard P. ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine- innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus. Journal Of Neuroscience 1989, 9: 3631-3637. PMID: 2552036, PMCID: PMC6569913, DOI: 10.1523/jneurosci.09-10-03631.1989.Peer-Reviewed Original ResearchConceptsARPP-21CAMP-dependent protein kinaseMolecular massMajor cytosolic substrateDopamine-innervated brain regionsAmino acid sequenceAmino acid sequencingProtein phosphorylationCytosolic substratesProtein kinaseAcid sequenceSeryl residuesHistidinyl residuesMolecular mechanismsBovine caudate nucleusPrimary structureNH2-terminalEdman degradationDopamine-innervated regionsPolypeptide chainAmino acid analysisCysteinyl residuesGas-phase sequencingPosition 55SDS-PAGE
1988
The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA
Gunther M, Tattersall P. The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA. FEBS Letters 1988, 242: 22-26. PMID: 3203742, DOI: 10.1016/0014-5793(88)80977-3.Peer-Reviewed Original Research
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