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Enrichment of glycopeptides for glycan structure and attachment site identification

descriptionPublicationkeyboard_double_arrow_right Article 18 Oct 2009 English Publisher:Springer Science and Business Media LLCJournal:Nature Methods, volume 6, pages 809-811 (issn: 1548-7091, eissn: 1548-7105,

Authors: Göran Larson; Elisabet Carlsohn; Ulla Rüetschi; Adnan Halim; Gunnar Brinkmalm; Camilla Hesse; Jonas Nilsson;

doi: 10.1038/nmeth.1392

pmid: 19838169

Enrichment of glycopeptides for glycan structure and attachment site identification

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Abstract

We present a method to enrich for glycoproteins from proteomic samples. Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds. Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification. We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.

Related Organizations

University of Gothenburg
Sweden
Sahlgrenska University Hospital
Sweden

Keywords

Proteomics, Glycosylation, Polysaccharides, Tandem Mass Spectrometry, Glycopeptides, Humans, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Cerebrospinal Fluid Proteins, Glycoproteins

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