Lectin techniques for glycoproteomics

Carol L. Nilsson

Research output: Contribution to journalReview article

5 Scopus citations

Abstract

One of the greatest challenges of the post-genomic and post-proteomic era is to understand the role of post-translational modifications in global biological systems. Protein glycosylation is one of the most frequent post-translational modifications but has been poorly studied in global proteomes because of analytical challenges associated with glycan structural characterization. In recent years, technical advances in the study of protein glycosylation have been achieved by the use of lectins as an enrichment tool for subproteomes modified by specific types of glycan structures. Many clinical biomarkers are glycoproteins and glycoproteomic studies that use lectin affinity techniques have been shown to have a superior ability to determine structure-specific biomarkers of disease. This article reviews key techniques and workflows, including the use of single-and multiple lectin columns and glycan detection by lectins.

Original languageEnglish (US)
Pages (from-to)248-256
Number of pages9
JournalCurrent Proteomics
Volume8
Issue number4
DOIs
StatePublished - Dec 1 2011

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Keywords

  • Affinity purification
  • Cancer
  • Glycoproteomics
  • Human disease
  • Lectins
  • Mass spectrometry
  • Microarrays
  • Protein separation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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