Lenoir G, Berthelon M C, Favre M C, de-Thé G
J Virol. 1976 Feb;17(2):672-4. doi: 10.1128/JVI.17.2.672-674.1976.
The Epstein-Barr virus-soluble (S) antigen extracted from RAJI cells was characterized by sucrose gradient centrifugation, gel filtration, and ion-exchange chromatography. The sedimentation coefficient was estimated to be 8.5S corresponding to a molecular weight of 180,000. The S antigen binds to DEAE-A25 ion exchanger from which it can be eluted with 0.3 M NaCl in Tris buffer (pH 7.2). All fractions which contained complement-fixing S antigen also inhibited the anticomplement immunofluorescence reaction as used to detect the Epstein-Barr virus-associated nuclear antigen. These results are consistent with the hypothesis that the S and Epstein-Barr virus-associated nuclear antigens are either a single antigen or that both activities are present on the same molecule.
从RAJI细胞中提取的爱泼斯坦-巴尔病毒可溶性(S)抗原,通过蔗糖梯度离心、凝胶过滤和离子交换色谱进行了特性分析。沉降系数估计为8.5S,对应分子量为180,000。S抗原与DEAE-A25离子交换剂结合,可用Tris缓冲液(pH 7.2)中的0.3M NaCl将其洗脱。所有含有补体结合性S抗原的组分也抑制了用于检测爱泼斯坦-巴尔病毒相关核抗原的抗补体免疫荧光反应。这些结果与以下假设一致,即S抗原和爱泼斯坦-巴尔病毒相关核抗原要么是单一抗原,要么两种活性存在于同一分子上。