Purification and partial characterization of L-fucose-specific lectin from fruit bodies of Peziza badia Merat.

An L-fucose-specific lectin from fruit bodies of the ascomycete Peziza badia Merat, was purified by affinity chromatography on agarose-coupled human ovariomucin (serotype H). This lectin binds L-fucose but is not specific to erythrocytes of blood group O(I), similarly to the lectin from Aleuria aurantia ascomycete. Unlike L-fucose-specific plant lectins, the lectin from P. badia binds with human thyroglobulin and mannofucogalactans of aphyllophoric fungi; this suggests that the lectin interacts with L-fucose located inside the polysaccharide chain of the glycoconjugates. Thus, the immunochemical properties of the lectins from P. badia and A. aurantia are similar.