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Interactions of Bowringia mildbraedii agglutinin with complex‐ and hybrid‐type glycans
Author(s) -
Chawla Davinder,
Animashaun Theresa,
Hughes R.Colin
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80079-v
Subject(s) - glycan , agglutinin , beta (programming language) , sequence (biology) , oligosaccharide , alpha (finance) , chemistry , glycopeptide , affinity chromatography , biochemistry , stereochemistry , glycoprotein , lectin , enzyme , mathematics , programming language , construct validity , statistics , antibiotics , computer science , psychometrics
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.