Carbohydrate binding specificity of immobilized Allomyrina dichotoma lectin II.

The carbohydrate binding specificity of Allomyrina dichotoma lectin II was investigated by analyzing the behavior of various complex type oligosaccharides and human milk oligosaccharides on an A. dichotoma lectin II-agarose column. Basically, the lectin interacts with the Gal beta 1—-4GlcNAc group. Substitution of their terminal galactose residues by Neu5Ac alpha 2—-6 will enhance their affinity to the lectin. By contraries, substitution at the C-2 or C-3 position of their terminal galactose with other sugars including sialic acid deprives their affinity to the lectin. With this characteristic, the immobilized lectin column can be used to separate complex type oligosaccharides with the Neu5Ac alpha 2—-6Gal beta 1—-4GlcNAc group from their isomeric oligosaccharides with the Neu5Ac alpha 2—-3Gal beta 1—-4GlcNAc group, where Neu5Ac is N-acetylneuraminic acid.