Lund G A, Salmi A A
J Gen Virol. 1981 Sep;56(Pt 1):185-93. doi: 10.1099/0022-1317-56-1-185.
The 79 000 mol. wt. measles virion membrane glycoprotein G has been isolated from purified measles virus. Ultracentrifugation of 2% Triton X-100-treated measles virus produced a soluble supernatant fraction containing both G and F, the other external viral membrane protein. Lentil lectin-Sepharose and Sephacryl S-300 column chromatography of this fraction gave a pure preparation of G protein. Sucrose density-gradient centrifugation and SDS-polyacrylamide gel electrophoresis revealed that G was isolated from the virion membrane in the form of a disulphide-linked dimer. Antiserum prepared against purified G reacted only with the G polypeptide of measles virus in a slab gel antibody overlay technique. The antiserum also exhibited haemagglutination inhibition, virus neutralization and haemolysis inhibition activities.
已从纯化的麻疹病毒中分离出分子量为79000的麻疹病毒颗粒膜糖蛋白G。对经2% Triton X-100处理的麻疹病毒进行超速离心，产生了一个可溶性上清液组分，其中含有G和F（另一种病毒外膜蛋白）。对该组分进行扁豆凝集素-琼脂糖凝胶柱层析和Sephacryl S-300柱层析，得到了G蛋白的纯制剂。蔗糖密度梯度离心和SDS-聚丙烯酰胺凝胶电泳显示，G是以二硫键连接的二聚体形式从病毒颗粒膜中分离出来的。在平板凝胶抗体覆盖技术中，针对纯化的G制备的抗血清仅与麻疹病毒的G多肽发生反应。该抗血清还表现出血凝抑制、病毒中和及溶血抑制活性。
