重组蛋白在大肠杆菌分泌表达的研究进展  

Advance in the secretory expression of recombinant protein in escherichia coli

作　　者：郑海洲[1] 刘晓志[1] 宋欣[1] 

机构地区：[1]华北制药集团新药研究开发有限责任公司,石家庄050015

出　　处：《天津药学》2009年第4期40-42,共3页Tianjin Pharmacy

摘　　要：长期以来,大肠杆菌是表达外源蛋白的首选表达系统,重组蛋白分泌表达与胞内表达相比有很大优越性,在细胞周质腔不仅能促进重组蛋白二硫键的形成及正确折叠,还能促进分泌蛋白的N-端加工。本文综述了近年来在大肠杆菌中表达可溶性外源蛋白的进展,目的是为了提高外源蛋白的生物活性。Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. Production of secretory proteins in escherichia coli provides several advantages over expression in the cytoplasm. Periplasm provides the oxidative en- vironment to facilitate correct disulfide bonding and protein folding. It also allows correct processing of N - terminal amino acid during secretion. This review discusses recent advances in secretory and extracellular production of recombinant proteins so as to improve the biologieal activity of the heterologous proteins.

关 键 词：大肠杆菌 分泌表达 重组蛋白 

分 类 号：Q591.2[生物学—生物化学]