Waniska R D, Kinsella J E
Int J Pept Protein Res. 1984 Jun;23(6):573-80. doi: 10.1111/j.1399-3011.1984.tb03129.x.
beta-Lactoglobulin was modified to various degrees with maltose or beta-cyclodextrin using the cyclic carbonate method and with glucosamine or glucosamine-octaose using the carbodiimide method. Up to 65% of the amino or the carboxyl groups of b-LG were glycosylated using the two methods, respectively. Up to 32 maltose residues were coupled to b-LG using the cyclic carbonate method while up to 16.6 glucosamine residues were coupled to b-LG using the carbodiimide method. This resulted because more than one disaccharide was attached to each group of b-LG that was modified. Even so, the coupling efficiency of the active compound was higher for the carbodiimide derivative than for the cyclic carbonate derivative. The electrophoretic analyses of the glycosylated proteins indicated that a heterogeneous population of protein molecules was formed during modification. The electrophoretic mobility of maltosyl-beta-lactoglobulin derivatives was essentially unchanged while the mobility of glucosaminyl-beta-lactoglobulin derivatives decreased as the extent of modification increased. The glycosylated proteins were suitable for studying their structural and functional properties.
使用环状碳酸酯法，β-乳球蛋白分别用麦芽糖或β-环糊精进行了不同程度的修饰；使用碳二亚胺法，β-乳球蛋白分别用氨基葡萄糖或氨基葡萄糖八糖进行了修饰。分别使用这两种方法时，高达65%的β-LG氨基或羧基被糖基化。使用环状碳酸酯法时，多达32个麦芽糖残基与β-LG偶联；使用碳二亚胺法时，多达16.6个氨基葡萄糖残基与β-LG偶联。这是因为在每一组被修饰的β-LG上连接了不止一个二糖。即便如此，活性化合物的偶联效率对于碳二亚胺衍生物而言高于环状碳酸酯衍生物。糖基化蛋白的电泳分析表明，修饰过程中形成了异质性的蛋白质分子群体。麦芽基-β-乳球蛋白衍生物的电泳迁移率基本不变，而氨基葡萄糖基-β-乳球蛋白衍生物的迁移率随着修饰程度的增加而降低。糖基化蛋白适合用于研究其结构和功能特性。
