摘要
采用琼脂糖凝胶CL-6B(Sepharose CL-6B)亲和层析以及Sephadex G-75凝胶分子筛等对大肠杆菌(Esche-richia coli,E.coli)半乳糖凝集素进行了纯化。结果显示,目标蛋白经简单的步骤即可以得到纯化,十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)及凝血实验证明纯化蛋白为E.coli半乳糖凝集素,蛋白提取回收率为11.4%。研究首次从E.coli蛋白提取液中分离得到纯的半乳糖凝集素,且此方法简单快捷,优越性明显。应用此方法将有利于微生物半乳糖凝集素的深入研究。
Sepharose CL-6B affinity chromatography and Sephadex G-75 gel chromatography were used to separate the galatose-binding lectin from E. coll. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and hemagglutination experiment showed that the obtained protein possessed the characteristic of hemagglutination and the target protein was E. coli galatose-binding lectin. The extraction rate was 11.4%.
出处
《生物加工过程》
CAS
CSCD
2009年第4期28-31,共4页
Chinese Journal of Bioprocess Engineering
基金
暨南大学自然科学基金资助项目(640073)
