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dc.contributor.authorMoh, Edward SX
dc.contributor.authorLin, Chi-Hung
dc.contributor.authorThaysen-Andersen, Morten
dc.contributor.authorPacker, Nicolle H
dc.date.accessioned2017-05-11T05:07:59Z
dc.date.available2017-05-11T05:07:59Z
dc.date.issued2016
dc.identifier.issn1044-0305
dc.identifier.doi10.1007/s13361-016-1378-0
dc.identifier.urihttp://hdl.handle.net/10072/336553
dc.description.abstractGlycosylation is known to play an important role in IgG antibody structure and function. Polymeric IgM, the largest known antibody in humans, displays five potential N-glycosylation sites on each heavy chain monomer. IgM can exist as a pentamer with a connecting singly N-glycosylated J-chain (with a total of 51 glycosylation sites) or as a hexamer (60 glycosylation sites). In this study, the N-glycosylation of recombinant pentameric and hexameric IgM produced by the same human cell type and culture conditions was site-specifically profiled by RP-LC-CID/ETD-MS/MS using HILIC-enriched tryptic and GluC glycopeptides. The occupancy of all putative N-glycosylation sites on the pentameric and hexameric IgM were able to be determined. Distinct glycosylation differences were observed between each of the five N-linked sites on the IgM heavy chains. While Asn171, Asn332, and Asn395 all had predominantly complex type glycans, differences in glycan branching and sialylation were observed between the sites. Asn563, a high mannose-rich glycosylation site that locates in the center of the IgM polymer, was only approximately 60% occupied in both the pentameric and hexameric IgM forms, with a difference in relative abundance of the glycan structures between the pentamer and hexamer. This study highlights the information obtained by characterization of the site-heterogeneity of a highly glycosylated protein of high molecular mass with quaternary structure, revealing differences that would not be seen by global glycan or deglycosylated peptide profiling.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.relation.ispartofpagefrom1143
dc.relation.ispartofpageto1155
dc.relation.ispartofissue7
dc.relation.ispartofjournalJournal of the American Society for Mass Spectrometry
dc.relation.ispartofvolume27
dc.subject.fieldofresearchAnalytical Chemistry not elsewhere classified
dc.subject.fieldofresearchAnalytical Chemistry
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchPhysical Chemistry (incl. Structural)
dc.subject.fieldofresearchcode030199
dc.subject.fieldofresearchcode0301
dc.subject.fieldofresearchcode0304
dc.subject.fieldofresearchcode0306
dc.titleSite-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorPacker, Nicki
gro.griffith.authorLin, Chi-Hung


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