Brief Communication abstract


Nature Methods 6, 809 - 811 (2009)
Published online: 18 October 2009 | doi:10.1038/nmeth.1392

Enrichment of glycopeptides for glycan structure and attachment site identification

Jonas Nilsson1, Ulla Rüetschi1, Adnan Halim1, Camilla Hesse1, Elisabet Carlsohn2, Gunnar Brinkmalm3 & Göran Larson1

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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.

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  1. Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, Sahlgrenska University Hospital, Gothenburg, Sweden.
  2. The Proteomics Core Facility, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  3. Department of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, University of Gothenburg, Sahlgrenska University Hospital, Mölndal, Sweden.

Correspondence to: Jonas Nilsson1 e-mail: jonas.nilsson@clinchem.gu.se



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