通过在大肠杆菌中共表达伴侣蛋白groES和groEL提高谷胱甘肽S-转移酶-P16（GST-p16）融合蛋白的溶解度

Increased solubility of glutathione S-transferase-P16 (GST-p16) fusion protein by co-expression of chaperones groes and groel in Escherichia coli.

作者信息

Luo Z H, Hua Z C

机构信息

Department of Biochemistry, Nanjing University, People's Republic of China.

出版信息

Biochem Mol Biol Int. 1998 Oct;46(3):471-7. doi: 10.1080/15216549800203992.

DOI:10.1080/15216549800203992

PMID:9818086

Abstract

Human cdk (cyclin dependent kinase) inhibitor p16 was fused with glutathione S-transferase (GST) and the GST-p16 fusion protein is under the control of T7 promoter. When expressed in E. coli BL21(DE3), most products existed in the form of insoluble inclusion bodies. When co-expressed with molecular chaperones E. coli GroESL, most GST-p16 products accumulated in the soluble form with a 5-6 fold increase in solubility. When coproduced with human protein disulfide isomerase (PDI), there was no improvement in the solubility of GST-p16 fusion protein.

摘要

人细胞周期蛋白依赖性激酶（cdk）抑制剂p16与谷胱甘肽S-转移酶（GST）融合，且GST-p16融合蛋白受T7启动子控制。当在大肠杆菌BL21(DE3)中表达时，大多数产物以不溶性包涵体的形式存在。当与分子伴侣大肠杆菌GroESL共表达时，大多数GST-p16产物以可溶形式积累，溶解度提高了5至6倍。当与人蛋白质二硫键异构酶（PDI）共同产生时，GST-p16融合蛋白的溶解度没有改善。