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dc.contributor.authorThaysen-Andersen, Morten
dc.contributor.authorWilkinson, Brendan L.
dc.contributor.authorPayne, Richard
dc.contributor.authorPacker, Nicolle H.
dc.date.accessioned2017-05-11T05:53:10Z
dc.date.available2017-05-11T05:53:10Z
dc.date.issued2011
dc.identifier.issn0173-0835
dc.identifier.doi10.1002/elps.201100294
dc.identifier.urihttp://hdl.handle.net/10072/336570
dc.description.abstractSite-specific characterisation of mucin-type O-linked glycosylation is an analytical challenge due to glycan heterogeneity, lack of glycosylation site consensus sequence and high density of occupied glycosylation sites. Here, we report the use of electron transfer dissociation (ETD) for the site-specific characterisation of densely glycosylated mucin-type O-linked glycopeptides using ESI-IT-MS/MS. Synthetic glycopeptides from the human mucin-1 (MUC-1) tandem repeat region containing a range of O-linked, tumour-associated carbohydrate antigens, namely Tn, T and sialyl T, with different glycosylation site occupancies and an increasing number of tandem repeats were studied. In addition, a glycopeptide from the anti-freeze glycoprotein of Antarctic and Arctic notothenoids, bearing four O-linked, per-acetylated T antigens was characterised. ETD MS/MS of infused or capillary LC-separated glycopeptides provided broad peptide sequence coverage (c/z·-type fragment ions) with intact glycans still attached to the Ser/Thr residues. Thus, the glycosylation sites were unambiguously determined, while simultaneously obtaining information about the attached glycan mass and peptide identity. Highly sialylated O-glycopeptides showed less efficient peptide fragmentation, but some sequence and glycosylation site information was still obtained. This study demonstrates the capabilities of ETD MS/MS for site-specific characterisation of mucin-type glycopeptides containing high-density O-linked glycan clusters, using accessible and relative low-resolution/low-mass accuracy IT MS instrumentation.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley - VCH Verlag GmbH
dc.relation.ispartofpagefrom3536
dc.relation.ispartofpageto3545
dc.relation.ispartofissue24
dc.relation.ispartofjournalElectrophoresis
dc.relation.ispartofvolume32
dc.subject.fieldofresearchAnalytical chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchChemical engineering
dc.subject.fieldofresearchcode3401
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode4004
dc.titleSite-specific characterisation of densely O-glycosylated mucin-type peptides using electron transfer dissociation ESI-MS/MS
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorPacker, Nicki


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