摘要
白细胞介素 1 1 (IL - 1 1 )是一种具有调节功能的蛋白质。一般采用含有IL - 1 1基因的硫氧还蛋白系统在重组大肠杆菌中来表达制备IL - 1 1融合蛋白 ,产物经金属鏊合层析进行初次分离。本文对融合蛋白IL - 1 1进行亲合纯化工艺研究 ,结果表明 ,IL - 1 1的纯度和回收率均达到较高的水平 。
Interleukin-11 (IL-11) is a kind of muti-function protein. Usually,people apply the thioredoxin fusion system containing the gene IL-11 to express IL-11 fusion protein in the E.coli and apply the immobilized metal affinity chromatography to purify the expression. In this paper,we study the affinity chromatography technics of the IL-11. The results show that both the purity and the rate of recovery reach the better level. It lays foundation for the followed purification.
出处
《化学工业与工程》
CAS
2003年第1期51-54,共4页
Chemical Industry and Engineering
关键词
纯化
白细胞介素11
重组大肠杆菌
金属鏊合亲和层析
IL-11
recombinant Easherichia coli
Immobilized metal ion affinity chromatography (IMAC)