Vasileva L, Nashkov D
Vet Med Nauki. 1975;12(2):11-5.
The protein fractions of the intact Newcastle disease virus as well as those of a disintegrated NDV (treatment with tween 80, ether and triton times 100) were separated through electrophoresis on polyacrylamid gel. Determined were the biologic activity, molecular weight and number of polypeptid chains of each fraction. It was found that 5 of the fractions obtained are composed of aggregates of 3 polypeptid chains, and 2 of the fractions represent single polypeptide chains. The haemagglutination and neuraminidase activity of the virus were found to be linked with the aggregates having molecular weight within the range of from 144,000 to 180,000 daltons. The complement-fixing activity observed is possessed by the single polypeptid having molecular weight of 62,000 daltons. It was demonstrated that the NDV strain that is not pathogenic for birds possesses a polypeptide with a molecular weight of 70,000 daltons, at is is not involved in the building of the protein aggregates.
通过聚丙烯酰胺凝胶电泳分离完整新城疫病毒以及经吐温80、乙醚和曲拉通X-100处理后的裂解新城疫病毒的蛋白质组分。测定了各组分的生物活性、分子量和多肽链数量。结果发现,所获得的5个组分由3条多肽链的聚集体组成,2个组分代表单条多肽链。发现病毒的血凝和神经氨酸酶活性与分子量在144,000至180,000道尔顿范围内的聚集体有关。观察到的补体结合活性由分子量为62,000道尔顿的单条多肽所具有。已证明对禽类无致病性的新城疫病毒株拥有一条分子量为70,000道尔顿的多肽,且该多肽不参与蛋白质聚集体的构建。