Lutsik M D, Antoniuk V A
Biokhimiia. 1982 Oct;47(10):1710-5.
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.
从金链花的树皮中纯化出了一种对L-岩藻糖具有特异性的新凝集素。纯化过程包括用硫酸铵沉淀（30 - 90%饱和度）、在pH 4.2下沉淀球蛋白组分、用瑞氏木素分级分离、在葡聚糖凝胶G - 100和二乙氨基乙基纤维素上进行色谱分离。SDS电泳显示出一条分子量为33,000的蛋白条带。天然凝集素的分子量约为130,000，因此表明该蛋白质分子具有四聚体结构。所获得的凝集素含有13.1%的碳水化合物；其氨基酸组成的特点是丝氨酸、苏氨酸、谷氨酸和天冬氨酸含量高，且缺乏胱氨酸和半胱氨酸。凝集素活性受到L-岩藻糖（2 mM）的抑制。凝集素能凝集天然人红细胞，对O(H)血型有偏好。在同一血型内观察到了各个红细胞样本血凝滴度的差异。
