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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

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Lectin Affinity Chromatography (LAC).

Brendan F O'Connor1,2,3, Donal Monaghan4, Jonathan Cawley4

  • 1School of Biotechnology, Dublin City University, Glasnevin, Dublin 9, Ireland. Brendan.oconnor@dcu.ie.

Methods in Molecular Biology (Clifton, N.J.)
|October 13, 2016
PubMed
Summary
This summary is machine-generated.

Lectin Affinity Chromatography (LAC) separates proteins with specific sugar attachments (glycans). This technique uses immobilized lectins to isolate glycoproteins and glycolipids, crucial for protein function and stability.

Keywords:
AffinityCon A sepharoseECL sepharoseFree haptenic sugarsFrontal affinity chromatographyGlycansGlycoproteinLectinRecombinant lectins

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Area of Science:

  • Biochemistry
  • Analytical Chemistry

Background:

  • Glycosylation, the binding of sugars (glycans) to proteins, is a critical post-translational modification.
  • Correct glycosylation is essential for protein folding, solubility, stability, and immunogenicity.

Purpose of the Study:

  • To describe the technique of Lectin Affinity Chromatography (LAC).
  • To highlight LAC's ability to separate various glycan-attached complexes.

Main Methods:

  • Utilizes immobilized lectins with specific affinity for particular sugar substrates.
  • Employs specific sugar elution to enhance separation specificity.
  • Operates under mild conditions to preserve biological integrity.

Main Results:

  • Successfully separates diverse glycan-attached complexes (glycoproteins and glycolipids).
  • Demonstrates good biological recoveries of target molecules.

Conclusions:

  • Lectin Affinity Chromatography (LAC) is an effective method for glycan analysis.
  • LAC provides a valuable tool for studying the role of glycosylation in protein function.