MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v01/MSV000082403/primary200OK0000ProteomicsZsuzsanna DarulaLTQ Orbitrap EliteHumanhttps://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=75e85180ea3740daadd024e11f9401b8zdarula@brc.huBiological Research CentreMassIVE13O-glycosylationN Acylneuraminate Glycohydrolases, Oligosaccharide Sialidase, peptides, determination, Artocarpus lectin jacalin, Exo-alpha-Sialidase, Exo alpha Sialidase, chemical analysis., Glycopeptide, Acylneuraminyl hydrolase, N-Acylneuraminate, heavy chain disease, Peptide, N-Acylneuraminate Glycohydrolases, polypeptide, peptide, Polypeptides, Oligosaccharide, peptido, HCD, Peptid, peptidos, ETD, Polypeptide, assay, Glycohydrolases, Chromatographies, jackfruit lectin jacalin, SialidaseGlycopeptide., jackfruit lectin jacalin, Artocarpus lectin jacalin0falseReproducibility of a WGA-Jacalin based affinity enrichment of O-glycopeptides from human serum tryptic digestHuman serum tryptic digest was enriched on a WGA-POROS affinity column collecting two glycopeptide fractions. The fractions were treated with neuraminidase and O-glycopeptides were isolated by a subsequent Jacalin affinity chromatography. Peptide mixtures were analyzed by LC/MS-MS applying HCD fragment ion dependent ETD analysis using an Orbitrap Elite mass spectrometer. Technical reproducibility was assessed using 3 parallel samples. Fri May 25 07:24:00 BST 2018MSV0000824039606