摘要
在猪口蹄疫病毒（FMDV）活性肽VP1融合蛋白基因工程菌E．coliC500构建成功的基础上，确定了融合蛋白的分子质量约为71．0ku．对于融合蛋白的提纯，确定了超声波破壁，尿素分级纯化，葡聚糖G－100柱层析，DEAE纤维素DE－52柱层析的方法，将目的蛋白提纯了6．75倍，SDS－PAGE呈一条带．并比较了融合蛋白的半乳糖苷酶反应（ONPG）和酶的温度敏感性等性质的变化．
A fusion protein of VP1 of Foot-and-Mouth Disease Virus jointed to the Cterminus of β-galastosidase was expressed in E. coli strain C500. The fusion protein with a molecular weight of about 70 ku, was extracted from bacteria cell by ultrasonication treatment combined with urea fractionation. The protein was further purified by molecularsieve chromatography on Sephadex G-100, ion-exchange chromatography on DE-52 to homogenous on SDS-polyacrylamide gel electrophoresis. The properties of the purified fusion protein were also studied.
出处
《复旦学报（自然科学版）》
CAS
CSCD
北大核心
1998年第4期501-504,共4页
Journal of Fudan University：Natural Science
基金
"八五"国家重点科技攻关项目
