Antonyuk V A
Division of Regulatory Cell Systems, Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Lvov, Ukraine.
Biochemistry (Mosc). 1997 Aug;62(8):841-4.
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.
通过在琼脂糖偶联的人卵巢粘蛋白（血清型H）上进行亲和层析，从子囊菌巴迪盘菌（Peziza badia Merat）的子实体中纯化出一种L-岩藻糖特异性凝集素。这种凝集素与L-岩藻糖结合，但与橙色盘菌（Aleuria aurantia）子囊菌的凝集素一样，对O(I)血型的红细胞不具有特异性。与L-岩藻糖特异性植物凝集素不同，巴迪盘菌的凝集素与人甲状腺球蛋白和无褶菌目真菌的甘露糖岩藻半乳聚糖结合；这表明该凝集素与糖缀合物多糖链内部的L-岩藻糖相互作用。因此，巴迪盘菌和橙色盘菌凝集素的免疫化学性质相似。
