人B淋巴细胞中爱泼斯坦-巴尔病毒/C3d补体受体的纯化：纯化蛋白的抗原性和功能特性
Purification of the Epstein-Barr virus/C3d complement receptor of human B lymphocytes: antigenic and functional properties of the purified protein.
作者信息
Nemerow G R, Siaw M F, Cooper N R
出版信息
J Virol. 1986 May;58(2):709-12. doi: 10.1128/JVI.58.2.709-712.1986.
The Epstein-Barr virus/C3d receptor (CR2) of human B lymphocytes was purified to homogeneity from Raji cells by immunoaffinity chromatography. The average yield of the 145-kilodalton receptor was 400 pmol (50 micrograms) per 10(10) cells, representing an approximate 75% recovery. The isolated 145-kilodalton protein was antigenically and functionally intact as it reacted with several anti-CR2 monoclonal antibodies and bound purified Epstein-Barr virus and C3d,g. These findings with the purified molecule provide an unequivocal demonstration of the dual receptor functions of this protein.
人B淋巴细胞的爱泼斯坦-巴尔病毒/C3d受体（CR2）通过免疫亲和层析从拉吉细胞中纯化至同质。每10¹⁰个细胞中145千道尔顿受体的平均产量为400皮摩尔（50微克），回收率约为75%。分离出的145千道尔顿蛋白质在抗原性和功能上均保持完整，因为它能与几种抗CR2单克隆抗体发生反应，并能结合纯化的爱泼斯坦-巴尔病毒和C3d,g。这些关于纯化分子的研究结果明确证明了该蛋白质的双重受体功能。
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