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1、AnImprovedProtocolforN-GlycosylationAnalysisofGel-SeparatedSialylatedGlycoproteinsbyMALDI-TOF/TOF112PiliangHao*,YanRen,YongmingXie1BeijinginstituteofGenomics,ChineseAcademyofScience,Beijing,China,2AppliedBiosystemsInc.(China),Shanghai,ChinaAbstractDiff
2、erentglycoformsofsomeproteinshavebeenidentifiedasdifferentialspotsforcertaindiseasesin2-DE,indicatingdisease-relatedglycosylationchanges.Itisroutinetodeterminethesite-specificglycosylationofnonsialylatedN-glycoproteinsfromasinglegelspot,butsomeobstacle
3、sstillexistinanalyzingsialylatedglycoproteinsduetothelabilityandhigherdetectionlimitofacidglycansinMALDI-TOF/TOFanalysis.Thus,wepresentanimprovedprotocolhere.TrypticglycopeptideswereseparatedandsubjectedtoMALDI-TOF/TOFanalysis,resultingintheidentificat
4、ionofsite-specificglycosylationofhigh-intensityglycopeptides.Sequentialdeglycosylationanddesialylationwereusedtoimprovetheidentificationofglycosylationsitesanddesialylatedglycans.Thesite-specificglycosylationoflargeglycopeptidesandlow-intensityglycopep
5、tideswasdeducedbasedonthemassesofglycopeptides,deglycosylatedpeptidesanddesialylatedglycans.Byapplyingitto2-DEseparatedhumanserum,thedifferenceofN-glycosylationwassuccessfullydeterminedfora1-antitrypsinbetweendifferentgelspots.Citation:HaoP,RenY,XieY(2
6、010)AnImprovedProtocolforN-GlycosylationAnalysisofGel-SeparatedSialylatedGlycoproteinsbyMALDI-TOF/TOF.PLoSONE5(11):e15096.doi:10.1371/journal.pone.0015096Editor:VladimirN.Uversky,UniversityofSouthFloridaCollegeofMedicine,UnitedStatesofAmericaReceivedAu
7、gust31,2010;AcceptedOctober20,2010;PublishedNovember29,2010Copyright:ß2010Haoetal.Thisisanopen-accessarticledistributedunderthetermsoftheCreativeCommonsAttributionLicense,whichpermitsunrestricteduse,distribution,andreproductioninanymedium,providedtheor
8、iginalauthorandsourcearecredited.Funding:ThisworkwassupportedbyResearchGrantfromBeijingInstituteofGenomics,ChineseAcademyofSciences.ItalsoreceivedinstrumentalsupportfromAppliedBiosystemsInc.(China).Thefundershadnoroleinstudydesign,datac
