Mohan S, Thambi Dorai D, Srimal S, Bachhawat B K
Biochem J. 1982 Apr 1;203(1):253-61. doi: 10.1042/bj2030253.
Interaction of the sialic acid-specific lectin carcinoscorpin with various sialoglycoproteins was studied by using radioiodinated lectin. The binding of carcinoscorpin was dependent not only on sialic acid content but also on the type of glycosidic linkage and form (branched or linear) of the carbohydrate chains. Carcinoscorpin has different classes of binding sites, and binding follows a phenomenon of positive co-operativity. The effect of Ca2+ concentration on the binding was studied, and the optimal concentration was found to be 0.02 M. Effect of pH, temperature and other bivalent metal ions are also reported. From haemagglutination- and precipitation-inhibition studies, it was concluded that carcinoscorpin has multispecificity towards acidic sugars, and its relation to the biological role of the lectin in the horseshoe crab is discussed.
利用放射性碘化凝集素研究了唾液酸特异性凝集素癌蟹素与各种唾液酸糖蛋白的相互作用。癌蟹素的结合不仅取决于唾液酸含量,还取决于碳水化合物链的糖苷键类型和形式(分支或线性)。癌蟹素有不同类型的结合位点,且结合呈现正协同效应。研究了Ca2+浓度对结合的影响,发现最佳浓度为0.02 M。还报道了pH、温度和其他二价金属离子的影响。通过血凝抑制和沉淀抑制研究得出结论,癌蟹素对酸性糖具有多特异性,并讨论了其与鲎中凝集素生物学作用的关系。