Lotan R, Debray H, Cacan M, Cacan R, Sharons N
J Biol Chem. 1975 Mar 10;250(5):1955-7.
Periodate oxidation of soybean agglutinin, a glycoprotein lectin, resulted in destruction of up to 5 out of the 9 mannose residues present in each of its subunits (MW 30,000) without any loss of hemagglutinating activity. The oxidation did, however, abolish the interaction of soybean agglutinin with concanvalin A, as measured by quantitative precipitation. Reduction with sodium [3-H]borohydride of soybean agglutinin in which 4 out of 9 mannose residues per subunit were oxidized, afforded a radioactive product which retained full hemagglutinating activity and was indistinguishable from the native lectin by gel filtration, gel electrophoresis, and affinity chromatography. These results establish that the integrity of the carbohydrate side chain of soybean agglutinin is not essential for the biological activity of the lectin, and suggest a general method for the preparation of radioactive glycoprotein lectins.
对大豆凝集素（一种糖蛋白凝集素）进行高碘酸盐氧化，导致其每个亚基（分子量30,000）中存在的9个甘露糖残基中多达5个被破坏，但血凝活性没有任何损失。然而，通过定量沉淀测量，这种氧化确实消除了大豆凝集素与伴刀豆球蛋白A的相互作用。用[3-H]硼氢化钠还原每个亚基中有4个甘露糖残基被氧化的大豆凝集素，得到一种放射性产物，该产物保留了完整的血凝活性，并且通过凝胶过滤、凝胶电泳和亲和色谱法与天然凝集素无法区分。这些结果表明，大豆凝集素碳水化合物侧链的完整性对于凝集素的生物活性不是必需的，并提出了一种制备放射性糖蛋白凝集素的通用方法。
