摘要
研究重组乙型肝炎病毒HBcAg蛋白表达条件和纯化方法,并对使用该方法纯化的抗原的理化性质和免疫原性进行分析。改变表达产物的培养和诱导表达条件,使用离子交换和分子筛进行层析纯化,用BALB/C小鼠进行动物效力试验。结果使蛋白以可溶形式表达,得到了纯度较高、抗原性较好、产生抗体滴度高的抗原蛋白。本试验介绍的HBcAg纯化方法较易扩大,可重复性好,为大量制备HBcAg蛋白提供了简洁高效的方法;并为以后进一步试验与其他抗原联合免疫制备有效的治疗性疫苗打下了良好的基础。
To explore the expressing condition and purification of the HBV core proteins and to investigate the antigenicity and immunogenicity of expressed proteins. To change the expressing condition of expressed proteins and to purify the protein by ion exchange chromatography the gel filtration, the immunization of BALB/C mice tested by ELISA method was carried out. The results showed that the bac teria protein became dissolved by changing the expressing condition, and the target protein becames very pure and could bring high level antibody to HBcAg. The method to purify HBcAg oculd be easy to enlarge and could have good repeatability, so it introduced a simple and high-performance method for us to produce vast protein. At the same time, it laid a foundation for further research and other antigen for ef fective therapy vaccine.
出处
《药物生物技术》
CAS
CSCD
2006年第3期187-191,共5页
Pharmaceutical Biotechnology