DSL contains two chains of 40 kDa and 46 kDa joined by
disulfide bonds. This lectin is free of a reported 32 kDa
contaminant protein. The carbohydrate binding site recognizes
(β-1,4) linked N-acetylglucosamine oligomers, preferring
chitobiose or chitotriose over a single N-acetylglucosamine
residue. This lectin binds well in the acidic pH range but its
affinity decreases above pH 8.0.
DSL also binds well to N-acetyllactosamine and oligomers
containing repeating N-acetyllactosamine sequences. A
branched pentasaccharide including two N-acetyllactosamine
disaccharides linked to mannose (β-1,6) and (β-1,2) was
reported to be the most potent inhibitor of agglutination.
Inhibiting/Eluting Sugar: Chitin Hydrolysate
|