Cumming D A
Carbohydrate Chemistry Group, Genetics Institute, Andover, MA 01810.
Dev Biol Stand. 1992;76:83-94.
The glycosylation of proteins is a complex biological pathway which is ordered and non-random. It is also a deterministic pathway dependent upon protein sequence, cellular phenotype, and the physiological environment. Two principal physiological roles have emerged within the past decade for protein-linked glycans: as recognition determinants and as modulators of various protein attributes such as bioactivity, pharmacokinetics, folding, and immunogenicity. All these attributes are crucial to development and application of protein-based pharmaceuticals. However, protein glycosylation represents a difficult structure/function problem since most glycoproteins exhibit microheterogeneity and oligosaccharides frequently contribute to this heterogeneity. Nevertheless, recent data suggest that different members of the heterogeneous ensemble exhibit distinguishable intrinsic properties, suggesting that the microheterogeneity of protein glycosylation represents a sophisticated mechanism of biological control.
蛋白质的糖基化是一条复杂的生物途径，它是有序且非随机的。这也是一条取决于蛋白质序列、细胞表型和生理环境的确定性途径。在过去十年中，蛋白质连接聚糖出现了两个主要生理作用：作为识别决定因素以及作为各种蛋白质属性（如生物活性、药代动力学、折叠和免疫原性）的调节剂。所有这些属性对于基于蛋白质的药物的开发和应用都至关重要。然而，蛋白质糖基化代表了一个困难的结构/功能问题，因为大多数糖蛋白表现出微不均一性，而寡糖常常导致这种不均一性。尽管如此，最近的数据表明，异质集合体的不同成员表现出可区分的内在特性，这表明蛋白质糖基化的微不均一性代表了一种复杂的生物控制机制。
