利用单克隆抗体免疫吸附剂大规模纯化爱泼斯坦-巴尔病毒膜抗原gp340
Large-scale purification of Epstein-Barr virus membrane antigen gp340 with a monoclonal antibody immunoabsorbent.
作者信息
Randle B J, Morgan A J, Stripp S A, Epstein M A
出版信息
J Immunol Methods. 1985 Feb 28;77(1):25-36. doi: 10.1016/0022-1759(85)90180-2.
A purification method has been elaborated to isolate Epstein-Barr (EB) virus membrane antigen, gp340, in milligram amounts. The gp340 was prepared from detergent extracts of B95-8 cells by affinity chromatography with a monoclonal antibody immunoabsorbent. Bound material was eluted and the eluate, consisting of 50% gp340, was then fractionated by gel filtration. The final gp340 product was antigenically active and 95% pure. The purification method was found to be rapid and reproducible with no loss of the ability of the immunoabsorbent to retain gp340 after repeated elution. The procedure provides suitable material to permit the detailed structural analysis of gp340 necessary for both vaccine design and for the investigation of the role of gp340 in immunity to EB virus infection.
已经精心设计了一种纯化方法，以毫克量分离爱泼斯坦-巴尔（EB）病毒膜抗原gp340。gp340是通过用单克隆抗体免疫吸附剂进行亲和色谱从B95-8细胞的去污剂提取物中制备的。结合的物质被洗脱，然后由50%的gp340组成的洗脱液通过凝胶过滤进行分级分离。最终的gp340产物具有抗原活性，纯度为95%。发现该纯化方法快速且可重复，免疫吸附剂在反复洗脱后保留gp340的能力没有损失。该程序提供了合适的材料，以便对gp340进行详细的结构分析，这对于疫苗设计以及研究gp340在抗EB病毒感染免疫中的作用都是必要的。
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