Abstract
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.
Highlights
The carbohydratebinding specificity of Allomyrina Recently, twonovel @-galactosebinding lectins (A110 A-I dichotoma lectin I1 was investigated by analyzing the and A110 A-11) were found in the hemolymph of the third behavior of various complex type oligosaccharides and human milk oligosaccharideson an A. dichotoma lectin 11-agarose column
Preliminary study of the binding specificity of an immobilized A110 A-I1 column with the use ofwell characterized oligosaccharides revealed an interesting characteristic of the column that some of the sialylated complex type sugar chains are tightlybound to the column
Since such characteristics seemed to be useful for the structural analysis of oligosaccharides, we have thoroughly investigated the behavior of known oligosaccharides in an AIIO A-11-agarose column in order to elucidate its binding specificity
Summary
EXPERIMENTALPROCEDURES the Neu5Aca2+3Ga1/31+4GlcNAc group, where Neu- Chemical and Enzymes-Uridine diphosphate [U-14CC]galactose. Because complex type sugar chains occupy the Oligosaccharidesand a Glycopeptide-Oligosaccharide XVI wapsrepared from the a-subunit of urinary human chorionic gonadotropin as described in a previous paper [9]. Synthetic GalPl4GlcNAc/31+ 4(Galpl+4GlcNAcpl+2)Manand Gal/31+4GlcNAc@l+6(Gal/31+ 4GlcNAcfll+Z)Man were kindly provided by Dr Tomoya Ogawa, majority of the three subgroups of asparagine-linked sugar Institute of Physical and Chemical Research, and by Dr Jorgen chains of glycoproteins, lectins which interact with @-galac- Lonngren, University of Stockholm, respectively. These oligosacchatosyl residues widely found in the outer chain moieties of complex type sugar chains areof particular use.
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