谷胱甘肽琼脂糖4B_

人NDRG1的GST融合表达、纯化及相互作用蛋白检测

http://www.100md.com 《第四军医大学学报》 2005年第20期

谷胱甘肽琼脂糖4B,,NDRG1；GST；基因表达；谷胱甘肽琼脂糖4B,0引言,1材料和方法,2结果,3讨论,【参考文献】

     GST fusion expression and purification of human NDRG1

    YANG Qian, ZHANG Jing, ZHANG YinYin, HE Peng, LIU XinPing, YAO LiBo, ZHAO HuiXian

    1College of Life Sciences, Northwest Scitech University of Agriculture and Forestry, Xian 712100, China, 2Department of Biochemistry and Molecular Biology, School of Basic Medicine, Fourth Military Medical University, Xian 710033, China

    【Abstract】 AIM: To better understand the function of NDRG1 and look for the interact protein through pulldown technic. METHODS: We digested the NDRG1 cDNA from the constructed vector NDRG1pPROEXHTb and transfered it into another vector pGEX4T1. After gene was sequenced, the recombinant vector NDRG1pGEX4T1 was transformed into E. coil DH5α and the strains highly expressing soluble GSTNDRG1 in LB medium containing ampicillin were obtained. The fusion protein was then purified by Glutathione Sepharose 4B and was incubated with HHCC. The interact protein with NDRG1 was observed by SDSPAGE. RESULTS: There was a new strip at Mr 4.0×104 when the purified protein and HHCC were incubated. CONCLUSION: The interact protein with NDRG1 is found in HHCC. ......

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