Glycosylation is a non-template-driven posttranslational modification during which linked-sugars and glycans are added to the nascent polypeptide. Over 70% of the eukaryotic proteome is thought to be glycosylated. It is now known that correct glycosylation is essential for the correct folding, solubility, stability, and immunogenicity of proteins. In this chapter, we describe the technique of lectin affinity chromatography (LAC), a procedure that has the ability to distinguish different glycans, which are attached to proteins or lipids, termed glycoproteins or glycolipids, respectively. This method utilizes different immobilized lectins that have affinity for specific sugar substrates, to separate a wide range of glycan-attached complexes (Ambrosi et al., Org Biomol Chem 3:1593-1608, 2005). To further enhance the specificity of LAC, a corresponding free sugar may be used to produce a specific elution. In general, the conditions under which lectin affinity chromatography operates are relatively mild resulting in good biological recoveries of the glycoproteins. © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Citation
Brendan F O'Connor, Donal Monaghan, Jonathan Cawley. Lectin Affinity Chromatography. Methods in molecular biology (Clifton, N.J.). 2023;2699:225-236
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PMID: 37647001
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