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

Abstract

Affinity chromatography on Bowittgitt trtifdbrurdii ngglutinin (BMA) Sepharose of glycopeptides confirmed a previous report using oligosaccharides (Animashaun, T. and Hughes, RC. (1989) was present. This moderate binding was not affected by substitution with N-acetylglucosaminc at C2 and C4, respectively, of the Manor143 and Mar@1+4 residues and BMA Sepharosc should prove to be a useful tool for the isolation of bisected or non-bisected hybrid-type glycans.Bowritrgia tttildbraedii agglutinin; Pectin; Carbohydrate binding specificity

Crystallization and preliminary X-ray analysis of the Man(α1-2)Man-specific lectin fromBowringia mildbraediiin complex with its carbohydrate ligand

“…The seeds of the Nigerian legume Bowringia milbraedii contain a Man/Glc-specific lectin (B. milbraedii agglutinin; BMA) that shows its highest affinity for the disaccharide Man(1-2)Man (Animashaun & Hughes, 1989;Chawla et al, 1992). The lectin reacts with human erythrocytes regardless of the blood type and can stimulate human and pig lymphocytes as effectively as concanavalin A or phytohaemagglutinin (Animashaun & Hughes, 1989).…”