摘要
为获得纯化的单抗以制备高效的单抗亲和层析柱,采用盐析、DEAE-Sephacel离子交换层析和Sephacryl S-_(300)凝胶过滤层析方法,对IgG亚类不同的抗人α-1和α-2a型基因工程干扰素(rHu-IFN-α)单抗进行纯化。结果,11D_2(IgG_(20))的纯度为81.5％,活性回收率为58.3％;17D_9(IgG_1)的纯度为91.1％,活性回收率为73.1％;1A_5(IgG_1)的纯度为93.7％,活性回收率为96.0％;1B_5(IgG_1)的纯度为97.0％,活性回收率为73.7％;27A_7(IgG_(2a))的纯度为93.4％,活性回收率为79.0％。
To obtain purified McAbs used for preparation of high efficiency McAb affinity chromatography column, various IgG subclasses of McAbs to human recombinant interferon-α_1, and α_2, were purified by precipitation, DEAE-Sephacel ion-exchange chromalography and Sephacryl S_(-300) gel filtration chromatography. The results showed that the purities of 11D_2 (IgG_(20)), 17D_9(IgG_1), 1A_5 (IgG_1), 1B_5(IgG_1) and 27A_7(IgG_(2a)) were 81.5%, 91. 1%, 93.7%, 97.0% and 93. 4%, respectively, and the recovery rates of their activity were 58. 3%, 73. 1%. 96. 0%. 73.74% and 70.0%
出处
《中国生物制品学杂志》
CAS
CSCD
1993年第2期66-69,共4页
Chinese Journal of Biologicals
关键词
单克隆抗体
层析
干扰素
提纯
Monoclonal antibody Chromatography Purification
