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Lectin Affinity Separation
Lectin Affinity Technology

Galanthus nivalis agglutinin
Lectin affinity separation is based on the ability of lectins to bind specifically to certain oligosaccharide structures on glycoconjugates. Different lectins display a variety of binding specificities. Lectins have been extensively used to purify glycoproteins, glycopeptides and oligosaccharides from all kinds of biological sources.

This technique is highly selective and thus provides a high purity target compound whilst the biological activity and natural glycosylation pattern is conserved due to the mild separation parameters.
Fig: GNA (Galanthus nivalis agglutinin), complex with 12 molecules of methylmannose
Process of Lectin Affinity Separation


Lectin Affinity Separation
  • A sample is applied that contains a target glycoprotein being complementary to the binding site of the immobilized lectin




  • The target glycoprotein specifically binds to the lectin





  • Unbound compounds and contaminants are washed out





  • The target glycoprotein is desorbed with a special elution buffer; the purified and concentrated product can be collected. The affinity matrix can be regenerated for further use.
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