CGGBP1蛋白在大肠杆菌中的表达及其纯化  

Expression and purification of CGGBP1 in E.coli

作　　者：杨芳[1] 张文红[1] 薛莉[1] 王琰[1] 夏琳[1] 白玉杰[1] 

机构地区：[1]第四军医大学全军基因诊断技术应用研究所

出　　处：《第四军医大学学报》2007年第12期1119-1121,共3页Journal of the Fourth Military Medical University

摘　　要：目的:对人CGGBP1蛋白进行原核表达及纯化,为进一步研究CGGBP1的生物功能奠定基础.方法:构建原核表达载体pRSETA/CGGBP1.在大肠杆菌BL21中诱导表达人CGGBP1蛋白,经Ni2+-NTA亲和层析纯化,利用链酶亲和素磁珠鉴定所表达纯化的蛋白能否和d(CGG)29重复序列双链DNA特异性结合.结果:诱导后表达得到CGGBP1蛋白,纯化得到的可溶性表达产物CGGBP1蛋白可以和d(CGG)29重复序列双链DNA特异性结合.结论:表达并纯化得到可溶性CGGBP1蛋白,为进一步研究CGGBP1的结构与功能奠定了必要的基础.AIM： To express and purify CGGBP1 for futher functional study. METHODS： The eDNA of CGGBP1 was amplified from eDNA library and cloned into the expression vector pRSET A. A recombinant plasmid containing CGGBP1 full length eDNA was constructed. After being transformed into E. coli BL21 （DE3）, CGGBP1 was expressed in E. coli after induction and the target protein was purified using Ni^2＋ -NTA chromatographic column. The binding of CGGBP1 to the double-stranded trinucleotide repeat sequence d （CGG） 29 was identified using Streptavidin-coated Magnetic Beads. RESULTS： The CGGBP1 protein was expressed in soluble form and bound specifically to the double-stranded trinueleotide repeat sequence d （CGG）29. CONCLUSION： The soluble CGGBP1 protein obtained will be useful to reseach its construction and functions in future.

关 键 词：ICGGBPl 基因表达 纯化 

分 类 号：Q75[生物学—分子生物学]