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Enrichment of glycopeptides for glycan structure and attachment site identification.

Journal article
Authors Jonas Nilsson
Ulla Rüetschi
Adnan Halim
Camilla Hesse
Elisabet Carlsohn
Gunnar Brinkmalm
Göran Larson
Published in Nature methods
Volume 6
Issue 11
Pages 809-11
ISSN 1548-7105
Publication year 2009
Published at Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine
Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 809-11
Language en
Links dx.doi.org/10.1038/nmeth.1392
Keywords attachment sites, glycoproteomics, sialic acid, enrichment, mass spectrometry, glycosylation, cerebrospinal fluid
Subject categories Neurochemistry, Clinical chemistry, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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.

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