Elucidation of the binding specificity of a concanavalin A-Sepharose column led to the possibility of the affinity chromatography of oligosaccharides and glycopeptides with the use of immobilized lectin columns. Subsequent addition of immobilized erythroagglutinating phytohaemagglutinin, Aleuria aurantia lectin, Datura stramonium agglutinin, Ricinus communis agglutinin and Allomyrina dichotoma agglutinin to the range of well characterized lectin columns has afforded a way to fractionate a mixture of N-linked oligosaccharides even to a single component.
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