抗菌肽Cecropin B-人溶菌酶重组蛋白的表达及纯化  

The Expression and Purification of a Novel Recombination Protein Cecropin B-Human Lysozyme

作　　者：翁婷[1] 贾信贵[1] 顾章鸿 沈晓东[1] 边六交[1] 

机构地区：[1]西北大学西部资源生物与现代生物技术教育部重点实验室,陕西西安710069

出　　处：《化学与生物工程》2007年第2期41-43,59,共4页Chemistry & Bioengineering

基　　金：陕西省科技攻关项目(2003K10-G58)

摘　　要：对抗菌肽Cecropin B-人溶菌酶(CB-hLy)的重组大肠杆菌进行了诱导表达,并对影响该重组蛋白表达的培养条件进行了优化,最后对表达出的重组蛋白进行了分离纯化。由上述方法得到的重组CB-hLy蛋白经十二烷基硫酸钠-聚丙烯酰胺电泳(SDS-PAGE)分析表明,其纯度可达90%,且具有良好的抑制真菌生长的生物活性。Induced with IPTG,a novel recombination protein Cecropin B-human lysozyme was expressed in recombinant E. coli and the influential culture conditions were optimized. After separation and purification,the recombination protein was analyzed by SDS PAGE.The results showed that the expressed CB-hLy protein had high biological activity to inhibit the growth of epiphyte with purity 90%.

关 键 词：抗菌肽 人溶菌酶 重组蛋白 表达 纯化 

分 类 号：Q785[生物学—分子生物学]