Purification and properties of an N‐acetylgalactosamine specific lectin from the plant pathogenic fungus Rhizoctonia solani

Abstract
A lectin was isolated from Rhizoctonia solani mycelium by affinity chromatography on gum arabic‐Sepharose. It is a dimeric protein composed of 2 identical subunits of 13 kDa with high contents of asparagine/ aspartic acid, valine, glycine, glutamine/glutamic acid and lysine. The R. solani agglutinin (RSA) exhibits specificity towards N‐acetylgalactosamine, and preferentially agglutinates human type A over type B and type O erythrocytes.