Wada Y, Nishikawa A, Okamoto N, Inui K, Tsukamoto H, Okada S, Taniguchi N
Osaka Medical Center, Japan.
Biochem Biophys Res Commun. 1992 Dec 15;189(2):832-6. doi: 10.1016/0006-291x(92)92278-6.
The structure of the defective transferrin in carbohydrate-deficient glycoprotein syndrome was characterized. Structurally abnormal sugar chains were not found in reversed phase chromatograms of pyridylaminated derivatives from the transferrin of two patients in different families. Electrospray ionization mass spectrometry of the whole transferrin molecules revealed an abnormal species that was smaller than normal tetrasialotransferrin by 2,200 daltons, just the size of the disialylated biantennary sugar chain. These data indicated that the disialotransferrin specifically found in this syndrome is missing either of two N-linked sugar chains, suggesting a metabolic error in the early steps of protein glycosylation.
对碳水化合物缺乏糖蛋白综合征中缺陷转铁蛋白的结构进行了表征。在来自不同家族的两名患者的转铁蛋白的吡啶氨基化衍生物的反相色谱图中未发现结构异常的糖链。对整个转铁蛋白分子进行电喷雾电离质谱分析,发现一种异常分子,其比正常的四唾液酸转铁蛋白小2200道尔顿,正好是二唾液酸化双天线糖链的大小。这些数据表明,在该综合征中特异性发现的二唾液酸转铁蛋白缺少两条N-连接糖链中的一条,提示在蛋白质糖基化早期步骤中存在代谢错误。