摘要
取本实验室制备的抗重组人γ干扰素单克隆抗体(rHu IFN-γ/McAb)A_3和B_3E_7粗制品(BALB/c小鼠腹腔分泌液),分别用饱和硫酸铵盐析法和葡萄球菌A蛋白(SPA)亲和层析法进行纯化。结果发现,虽两者都能部分纯化A_3和B_3E_7-McAb,但后者(SPA亲和层析法)的纯化效果比前者(硫酸铵盐析法)好。纯化后的产品经冷冻干燥后置低温贮存,其活性(抗体滴度)不受影响.
Monoclonal antibodies (MAba)A5 and B3 E7, specific for recombinant human ga-mma-interferon (rHuIFN-r) from BALB/c mouse ascitIc fluid were prepared in our laboratory. The crude agents have been purifIed by saturated (NH4)2SO4 precipitation methed and SPA-sepharose affinity chromatography, respectively.The experimental results indicated that both methods could achieve partial purification of anti-rHuIFN-r MAb, but a rather greater yield of the active MAb could be obtained with SPA-sepharose chromatography. The activity of the purified rHuIFN-r MAb was quite stable and was not affected by lyophilization.
出处
《上海免疫学杂志》
CSCD
北大核心
1989年第3期133-136,共4页
Shanghai Journal of Immunology
