About the Lectin
A lectin found primarily in the roots of Bryonia dioica is a potent non-specific hemagglutinin 1 . The lectin is most abundant in the root stocks, but it has been found in other parts of the plant as well. Similar to Aegopodium podagraria (APP), BDA is readily inhibited by several simple sugars, especially GalNAc, lactose, and melibiose. Although BDA is inhibited by simple sugars, it does not bind to these same sugars bound to an affinity matrix. Due to this finding, an immobilized glycoprotein has been used to isolate the purified lectin. Crude root extracts have the same carbohydrate specificity as the purified lectin. BDA is not blood group specific but it does react stronger with trypsin treated erythrocytes than with untreated cells. Purified BDA is a dimeric glycoprotein composed of two dissimilar subunits. The lectin dissociates in the presence of reducing agents such as mercaptoethanol, but remains intact in 8M urea. BDA and APP exhibit similar carbohydrate specificities, but they differ with regard to glycoprotein binding properties. BDA has also been applied to typing β-hemolytic streptococci 2 .
- Peumans, W. J., et al. (1984) Planta. 160 : 222-228.
- Kellens, J. T.C., et al. (1993) J. Med. Microb 39 : 440-445.
|Buffer||0.01M Phosphate – 0.15M NaCl, pH 7.2-7.4.|
|Activity||Less than 0.5 μg/ml will agglutinate human type O erythrocytes.|
|Inhibitory Carbohydrate||N-acetyl‑D‑galactosamine > Lactose > Melibiose.|
|Molecular Weight||MW=61,000 by SDS-PAGE. Under reducing conditions two bands of 30,000 and 32,000 appear.|