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

FEBS Letters

Hughes, R.Colin¹  Animashaun, Theresa¹  Chawla, Davinder¹ 

[1] Nationial Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK

关键词: Bowringia mildbraedii agglutinin;    Lectin: Carbohydrate binding specificity;    BMA;    Bowringia mildbraedii agglutinin;    Con A;    Concanavalin A;    endo H;    endoglycosidase H;    endo D;    endoglycosidase D;    GlcNAcot;    N-acetylglucosaminitol;   

DOI  :  10.1016/0014-5793(92)80079-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown