【摘要】 将牛乳铁蛋白素(lactoferricin B)基因克隆到表达载体pET28a后,转化到BL21大肠杆菌表达系统,筛选表达温度和诱导剂IPTG的浓度,使其在原核表达系统中表达,将诱导表达的产物进行Tricine-SDS-PAGE蛋白电泳及抑菌活性检测,证明该表达产物是乳铁蛋白素。实验结果表明,LactoferricinB基因能够在原核表达系统中表达,表达量约占细菌总蛋白的21%,而且表达的蛋白质具有生物学活性。更多还原

【Abstract】 After cloning into the expression vector pET28a, the lactoferricin B gene was transformed into BL-21 E.coli prokaryotic expression system. By selecting expression temperature and IPTG concentration, lactoferricin B gene was expressed at high level in prokaryotic cells. The expression of lactoferricin B was detected by tricine-SDS-PAGE protein electrophoresis and functional test, and it was proved to be the lactoferricin B. The result also showed that the gene of lactoferricin B can be highly expressed in prokaryotic expression system, and the expression product accounts for about 21% of total bacterial proteins with biology activity.更多还原