Interactions of Bowringia mildbraedii agglutinin with complex‐ and hybrid‐type glycans

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Abstract
Affinity chromatography on Bowringia mildbraedii agglutinin (BMA) Sopharose of glycopeptides confirmed a previous report using oligo‐saccharides (Animashaun, T. and Hughes, R.C. (1989) J. Biol. Chem. 264,4657–4663) that high affinity binding requires the sequence Manα1→2 Manα1→6 Manα1→6 Manβ1→4. However, moderate binding was still exhibited by structures lacking this sequence provided the oligosaccharide core sequence Manα1→3[Manα1→6]Manβ1→4GlcNAc was present. This moderate binding was not affected by substitution with N‐acetylgluco‐samine at C2 and C4, respectively, of the Manα1→3 and Manβ1→4 residues and BMA Sepharose should prove to be a useful tool for the isolation of bisected or non‐bisected hybrid‐type glycans.