Abstract
Publisher Summary This chapter describes a high throughput purification protocol and methods to study the binding activity of psathyrella velutina lectin (PVL) toward monosaccharides, oligosaccharides, or glycoproteins and elucidates its specificity toward NeuAc-containing glycoconjugates by comparing it with other NeuAc-binding lectins. PVL has been used as an N -acetylglucosamine (GlcNAc)-specific reagent for the detection of glycoconjugates. Chemically-labeled PVL could detect sialyl residues and differentiate them from GlcNAc residues when used in combination with the glycosidase treatment of glycoconjugates. The binding activity of PVL for acidic polysaccharides, such as heparin and polygalacturonic acid, was blocked specifically by the biotinylation of PVL possessing GlcNAc/NeuAcbinding activity. PVL-Sepharose is also a useful tool for the separation of glycoconjugates containing NeuAc or terminal GlcNAc residues from others in terms of the number or linkage of these sugar residues.
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