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Related Concept Videos

Affinity Chromatography01:03

Affinity Chromatography

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Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
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The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
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Selectins01:25

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Updated: Jul 17, 2025

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.

Brendan F O'Connor1, Donal Monaghan1, Jonathan Cawley2,3

  • 1School of Biotechnology, Dublin City University, Dublin, Ireland.

Methods in Molecular Biology (Clifton, N.J.)
|August 30, 2023
PubMed
Summary
This summary is machine-generated.

Lectin affinity chromatography (LAC) separates glycoproteins and glycolipids by exploiting lectin-carbohydrate interactions. This method uses immobilized lectins to purify specific glycan-attached molecules under mild conditions.

Keywords:
AffinityCon A Sepharose®Free haptenic sugarsFrontal affinity chromatographyGlycansGlycoproteinLectinRecombinant lectins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycobiology

Background:

  • Glycosylation is a crucial posttranslational modification affecting over 70% of proteins.
  • Proper glycosylation is vital for protein folding, solubility, stability, and immunogenicity.
  • Glycoproteins and glycolipids are essential biological molecules with diverse functions.

Purpose of the Study:

  • To describe the technique of lectin affinity chromatography (LAC).
  • To highlight LAC's ability to distinguish and separate various glycan structures.
  • To present LAC as a method for purifying glycoproteins and glycolipids.

Main Methods:

  • Utilizes immobilized lectins with specific affinities for distinct sugar substrates.
  • Employs lectin-carbohydrate interactions for separation of glycan-attached complexes.
  • Can incorporate specific sugar elutions to enhance purification specificity.

Main Results:

  • LAC effectively separates a wide range of glycan-attached complexes.
  • The method operates under mild conditions, ensuring good biological recovery.
  • Distinguishes between different glycans attached to proteins or lipids.

Conclusions:

  • Lectin affinity chromatography is a powerful technique for purifying and analyzing glycoproteins and glycolipids.
  • LAC offers high specificity and efficiency in glycan-based separations.
  • The method is suitable for preserving the biological activity of purified molecules.