摘要
以包含体形式由大肠杆菌表达的基因重组人白细胞介素２（ｒｈＩＬ－２），经纯化后其纯度已达９５％以上［１］。我们采用免疫印迹法和部分氨基酸序列分析等较特异、敏感和准确的检测手段，对纯化ｒｈＩＬ－２的抗原特性和Ｎ末端１５个氨基酸序列进行检测分析，获得了满意的结果。
Human recombinant interleukin-2 (rhIL-2) in the form of inclusion bodies derived from E. coli was purified with the homogeneity of more than 95%. The results of the antigenicity and fifteen amino acids of N -terminal analyses of the purified rhIL-2 by using specific, sensitive and accurate techniques of Western blot and the partial annno acid sequencing were satisfactory.
出处
《第二军医大学学报》
CAS
CSCD
北大核心
1994年第6期525-527,共3页
Academic Journal of Second Military Medical University
