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Related Experiment Videos

Solid-phase extraction of N-linked glycopeptides.

Yuan Tian1, Yong Zhou, Sarah Elliott

  • 1Institute for Systems Biology, Seattle, Washington 98103, USA.

Nature Protocols
|April 5, 2007
PubMed
Summary
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This study presents a novel method for identifying N-linked glycosylation sites on proteins. The technique uses solid-phase extraction and mass spectrometry to detect hundreds of glycoproteins and their glycosylation sites.

Area of Science:

  • Biochemistry
  • Proteomics
  • Glycobiology

Background:

  • Protein glycosylation is a key post-translational modification.
  • N-linked glycosylation is crucial in tumorigenesis and cancer biomarkers.
  • Identifying glycosylation sites is vital for understanding protein function.

Purpose of the Study:

  • To develop a robust protocol for N-linked glycopeptide enrichment.
  • To enable site-specific identification of N-linked glycosylation.
  • To facilitate quantitative analysis of glycopeptides.

Main Methods:

  • Solid-phase extraction of N-linked glycopeptides via carbohydrate oxidation and immobilization.
  • Optional stable isotope labeling of glycopeptides.
  • Peptide release using peptide-N-glycosidase.

Related Experiment Videos

  • Tandem mass spectrometry for identification.

    • Main Results:

    • Identification of hundreds of N-linked glycoproteins in a single analysis.
    • Precise localization of N-linked glycosylation sites (N-glycosites).
    • Quantification of relative glycopeptide abundance.

    Conclusions:

    • The described protocol offers an efficient method for N-linked glycopeptide analysis.
    • This technique aids in the discovery of cancer biomarkers and therapeutic targets.
    • The method provides comprehensive insights into protein glycosylation patterns.