hIL-3突变体在大肠杆菌中的表达及纯化  

Purification of hIL-3 mutant highly expressed in E.coli

作　　者：王燕[1] 毛琼国[1] 万瑛[1] 纪贤文[1] 刘昕[1] 

机构地区：[1]第三军医大学基础医学部分子遗传学教研室,重庆400038

出　　处：《第三军医大学学报》2000年第1期33-35,共3页Journal of Third Military Medical University

摘　　要：目的 :将天然型hIL 3蛋白经定点突变为hIL 3突变体蛋白 ,并在大肠杆菌中表达及纯化。方法 :超声破碎细菌得到包涵体 ,经DEAEFastFlow,SephaecrylS 200HR等层析步骤纯化。结果 :经以上一系列纯化 ,得到的人IL 3突变体蛋白纯度达90 % ,比活性为7.3×104 U/ml ,总回收率为100 %。结论 :突变体hIL 3在大肠杆菌中得到高效表达 ,并获得高纯度、高活性的hIL 3蛋白。Objective: To purify hIL 3 mutant from E.coli. Methods: Inclusion bodies were collected after the breakage of bacteria. Then the pure hIL 3 mutant was obtained by DEAE sepharose fast flow and sephacry1S 200HR. Results: The purity of the product was about 90%. In vitro test of the TF 1 cells showed the relative activity of hIL 3 mutant was 7.3×104 unit/ml. The total recovery of this protocol was approximately 100%.Conclusion:hIL 3 mutant is highly expressed in E.coli. hIL 3 protein with high purity and activity is obtained.

关 键 词：hIL-3突变体 大肠杆菌 纯化 免疫分子遗传学 

分 类 号：R392.13[医药卫生—免疫学] R378.21[医药卫生—基础医学]