Interactions of Bowringia mildbraedii agglutinin with complex- and hybrid-type glycans.
Affinity chromatography on Bowringia mildbraedii agglutinin (BMA) Sepharose of glycopeptides confirmed a previous report using oligosaccharides (Animashaun, T. and Hughes, R. C. (1989) J. Biol. Chem. 264,4657-4663) that high affinity binding requires the sequence Man alpha 1---2 Man alpha 1----6 Man alpha 1----6 Man beta 1----4. However, moderate binding was still exhibited by structures lacking this sequence provided the oligosaccharide core sequence Man alpha 1----3[Man alpha 1----6]Man beta 1----4GlcNAc was present. This moderate binding was not affected by substitution with N-acetylglucosamine at C2 and C4, respectively, of the Man alpha 1----3 and Man beta 1----4 residues and BMA Sepharose should prove to be a useful tool for the isolation of bisected or non-bisected hybrid-type glycans.
Chawla
D
D
National Institute for Medical Research, The Ridgeway, Mill Hill, London, UK.
Animashaun
T
T
Hughes
R C
RC
D000373:Agglutinins / Q000737:chemistry / Q000378:metabolism*; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D007887:Fabaceae / Q000378:metabolism*; D006020:Glycopeptides / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D010946:Plants, Medicinal; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*
D000373:Agglutinins; D006020:Glycopeptides; D009844:Oligosaccharides; D011134:Polysaccharides