摘要
重组人白细胞介素-6(rhIL-6)在工程菌pBV220/rhIL-6/DH5a中以包涵体形式高效表达。rhIL-6经过工程菌体破碎、包涵体分离及抽提、复性、色谱分离后得到高度纯化。纯化产物纯度95%。
rhIL 6 was highly expressed in E.coli in the form of inclusion bodies.rhIL 6 was pruified to homogeneity with cell disruption,inclusion bodies extraction and solubilization,renaturation and chromatography separation procedures.The purified protein showed good bioactivity in vitro and its purity is greater than 95%.
出处
《微生物学免疫学进展》
1999年第1期47-50,共4页
Progress In Microbiology and Immunology