渗透休克法从大肠杆菌中提取GST-Tα1-TP5融合蛋白

Release of GST-thymosin α 1-thymopentin fusion protein by osmotic shock from escherichia coli

目的:从大肠杆菌中选择性抽提GST-Tα1-TP5融合蛋白。方法:采用渗透休克法从大肠杆菌中提取GST-Tα1-TP5融合蛋白,优化操作条件,并与超声破碎法进行比较。结果:优化后的渗透休克法从大肠杆菌提取GST-Tα1-TP5融合蛋白可使杂蛋白量含量相对超声破碎法降低一个数量级。结论:渗透休克法可高效提取大肠杆菌表达的GST-Tα1-TP5融合蛋白。

Objective： To selectively extract GST-thymosin α 1-thymopentin fusion protein from E. coll. Methods： Osmotic shock method was used to extract GST-thymosin al-thymopentin fusion protein from E. coli. After the optimization of the operating conditions, it would be compared with the sonication method. Results： Compared with the sordcation method, the optimized osmotic shock method used to extract GST-thymosin al-thymopentin fusion protein from E. coil makes hybridprotein content reduce an order of magnitude. Conclusion： Osmotic shock method can efficiently extract GST-thymosin α1-thymopenfin fusion protein.