| Abstrakt: |
A new lectin specific towards L-fucose has been purified from the bark of Laburnum anagyroides. The purification procedure included precipitation with ammonium sulfate (30-90% saturation), precipitation of the globuline fraction at pH 4.2, fractionation with rivanol, chromatography on Sephadex G-100 and DEAE-cellulose. Electrophoresis in SDS revealed one protein band with molecular weight of 33,000. The molecular weight of the native lectin is about 130,000, thus suggesting a tetrameric structure of the protein molecule. The lectin obtained contains 13.1% of carbohydrates; its amino acid composition is characterized by a high content of serine, threonine, glutamic and aspartic acids and by a lack of cystine and cysteine. The lectin activity is inhibited by L-fucose (2 mM). Lectin agglutinates native human erythrocytes with a preference for the O(H) blood group. The differences in the titre of hemagglutination of individual erythrocyte samples within a unique blood group were observed. |
