Abstract
Leaves of Bauhinia monandra Kurz. (pata-de-vaca, pulse) contain a relatively high concentration of a galactose-specific lectin (BmoLL). More than 2 mg of BmoLL were obtained from 5 g of leaf powder when a 10% (w/v) extract was submitted to 60% ammonium sulphate fractionation followed by guar gel affinity chromatography. The purified lectin ran slowly as a single broad band on non-denaturing electrophoresis. Under denaturing and reducing conditions, it appeared as a major subunit of apparent molecular weight 33 kDa, positive to carbohydrate staining, and a non-glycosylated polypeptide (26 kDa). Column fractions containing the peak of BmoLL eluted from the affinity chromatography, each containing the 33 and 26 kDa polypeptides. The highest agglutination activity of BmoLL was found with glutaraldehyde-treated rabbit erythrocytes; fresh and glutaraldehyde-treated human erythrocytes of blood groups B and AB were also agglutinated, whereas those from groups A and O were not. Copyright © 2000 John Wiley & Sons, Ltd.
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