Fleissner E
J Virol. 1971 Nov;8(5):778-85. doi: 10.1128/JVI.8.5.778-785.1971.
Gel filtration of avian tumor virus proteins in 6 m guanidine hydrochloride clearly resolved seven major protein species. The antigenic activity of these proteins was recovered in good yield after removal of the denaturing solvent, permitting a correlation of specific polypeptides with the principal antigens of the virion. Two of the proteins, of molecular weights 70,000 and 32,000, contain carbohydrate and are situated on the viral membrane, as shown by their being accessible in the intact virus to specific antibodies. Four proteins, with molecular weights (in guanidine) of 27,000, 19,000, 15,000, and 12,000, have different group-specific (gs) antigens and are enclosed within the viral membrane. The smallest protein, with a molecular weight of 10,000, has not previously been described; it is not detectable with antisera and possesses a mobility identical to that of one gs protein when subjected to electrophoresis in polyacrylamide gels in the presence of sodium dodecyl sulfate. Of the proteins lacking carbohydrate, three are present in the virion in a molecular ratio of 2:2:1, and the two others, present in almost equal amount, are rich in lysine and arginine.
在6M盐酸胍中对禽肿瘤病毒蛋白进行凝胶过滤，清晰地分离出七种主要蛋白质。去除变性溶剂后，这些蛋白质的抗原活性得以良好恢复，从而能够将特定多肽与病毒粒子的主要抗原联系起来。其中两种蛋白质，分子量分别为70,000和32,000，含有碳水化合物，位于病毒膜上，完整病毒中的这些蛋白质可与特异性抗体结合，这表明了它们的位置。四种蛋白质，在胍中的分子量分别为27,000、19,000、15,000和12,000，具有不同的群特异性（gs）抗原，被包裹在病毒膜内。最小的蛋白质，分子量为10,000，以前未曾描述过；用抗血清检测不到它，在十二烷基硫酸钠存在下进行聚丙烯酰胺凝胶电泳时，它的迁移率与一种gs蛋白相同。在不含碳水化合物的蛋白质中，三种以2:2:1的分子比例存在于病毒粒子中，另外两种含量几乎相等，富含赖氨酸和精氨酸。
