Chan S K, Rees D C
J Biol Chem. 1976 Jan 25;251(2):471-6.
Two glycopeptides present in equal amounts were isolated from a pronase digest of alpha1-protease inhibitor of human plasma by gel filtration on Sephadex G-50 and chromatography on DEAE-cellulose. The carbohydrate side chains in both glycopeptides are linked through asparaginyl residues. The glycopeptides were digested sequentially with specific glycosidases; and after each step, the released sugars as well as the composition of the residual peptides were determined. The linear structures of these glycopeptides deduced from these data are shown below. Based on the total carbohydrate content of the intact protein and with these structural data, it is postulated that 4 oligosaccharide units are attached to 1 molecule of the protein; 2 of these were represented as in Equation 1, the other 2 as in Equation 2.
通过在葡聚糖凝胶G - 50上进行凝胶过滤以及在二乙氨基乙基纤维素上进行色谱法,从人血浆α1 - 蛋白酶抑制剂的链霉蛋白酶消化物中分离出了两种等量的糖肽。两种糖肽中的碳水化合物侧链均通过天冬酰胺残基相连。这些糖肽依次用特定的糖苷酶进行消化;在每一步之后,测定释放出的糖以及残留肽的组成。从这些数据推导得出的这些糖肽的线性结构如下所示。根据完整蛋白质的总碳水化合物含量以及这些结构数据,推测1分子该蛋白质连接有4个寡糖单元;其中2个如等式1所示,另外2个如等式2所示。