Anttonen O, Jokinen M, Salmi A, Vainionpää R, Gahmberg C G
Biochem J. 1980 Jan 1;185(1):189-94. doi: 10.1042/bj1850189.
Measles virus was propagated in VERO cells and purified from the culture supernatants by two successive tartrate-density-gradient centrifugations. Surface carbohydrates were labelled both in vitro and in vivo with 3H after treatment with galactose oxidase/NaB3H4 or with [3H]glucosamine. The major labelled glycoprotein in measles virions had a mol.wt. of 79 000. After labelling with periodate/NaB3H4, which would result in specific labelling of sialic acid residues, the 79 000-mol.wt. glycoprotein was very weakly labelled. This suggests that there is no or a very low amount of sialic acid in the virions. Further analysis of the glycoprotein showed that galactose is the terminal carbohydrate unit in the oligosaccharide, and the molecular weight of the glycopeptide obtained after Pronase digestion is about 3000. The oligosaccharide is attached to the polypeptide through an alkali-stable bond, indicating a N-glycosidic asparagine linkage.
麻疹病毒在非洲绿猴肾细胞（VERO细胞）中繁殖，并通过两次连续的酒石酸盐密度梯度离心从培养上清液中纯化出来。在用半乳糖氧化酶/硼氢化钠（NaB3H4）或[3H]葡糖胺处理后，表面碳水化合物在体外和体内均用3H进行标记。麻疹病毒粒子中主要的标记糖蛋白分子量为79000。在用高碘酸盐/硼氢化钠（NaB3H4）标记后，这会导致唾液酸残基的特异性标记，分子量为79000的糖蛋白被标记得非常弱。这表明病毒粒子中不存在或存在极少量的唾液酸。对该糖蛋白的进一步分析表明，半乳糖是寡糖中的末端碳水化合物单元，经链霉蛋白酶消化后得到的糖肽分子量约为3000。寡糖通过碱稳定键与多肽相连，表明是N-糖苷天冬酰胺连接。
