Spik G, Coddeville B, Montreuil J
Université des Sciences et Techniques de Lille Flandres-Artois, Laboratoire de Chimie Biologique (Unité Associée au CNRS No. 217), Villeneuve-d'Ascq, France.
Biochimie. 1988 Nov;70(11):1459-69. doi: 10.1016/0300-9084(88)90283-0.
In order to establish relationships between glycan structure and biological activity and to answer the question: Are glycans markers of evolution?, the authors undertook a comparative study of the glycan primary structures of different transferrins (sero-, lacto- and ovotransferrins) from several species. By associating permethylation--mass spectrometry and 1H NMR spectroscopy, the primary structure of the following transferrin glycans were determined: human, bovine, hen, horse, marsupial, mouse, rabbit, rat and sheep serotransferrins; human, mouse, bovine and goat lactotransferrins; hen and turkey ovotransferrins. The results obtained led to the conclusion that transferrin glycans are specific for each transferrin and, for a given transferrin, specific to the species. No relationship could be established a priori between primary structure and function of transferrin glycans.
为了建立聚糖结构与生物活性之间的关系,并回答“聚糖是进化的标志吗?”这一问题,作者对来自多个物种的不同转铁蛋白(血清转铁蛋白、乳铁蛋白和卵转铁蛋白)的聚糖一级结构进行了比较研究。通过结合全甲基化-质谱和1H NMR光谱,确定了以下转铁蛋白聚糖的一级结构:人、牛、鸡、马、有袋动物、小鼠、兔、大鼠和绵羊的血清转铁蛋白;人、小鼠、牛和山羊的乳铁蛋白;鸡和火鸡的卵转铁蛋白。所得结果得出结论,转铁蛋白聚糖对每种转铁蛋白具有特异性,并且对于给定的转铁蛋白,对物种具有特异性。转铁蛋白聚糖的一级结构与功能之间无法预先建立关系。