Purification and Partial Characterization of L-Fucose-Specific Lectin from Fruit Bodies of Peziza badia Merat.

V. A. Antonyuk¹

¹Division of Regulatory Cell Systems, Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, ul. Dragomanova 14/16, Lvov, 290005, Ukraine.

Submitted January 5, 1997; revision submitted April 28, 1997.

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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.

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KEY WORDS: L-fucose-specific lectin, Peziza, Aleuria, Laburnum anagyroides, Tetragonolobus purpureus, purification, properties, carbohydrate specificity, comparative characteristics.

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