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人尿激酶原与大肠杆菌硫氧还蛋白的融合表达。

Fusion expression of human pro-urokinase with E. coli thioredoxin.

作者信息

Sun A L, Hua Z C, Yao J, Yang Y H, Yin D Q

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):479-86. doi: 10.1080/15216549800204002.

Abstract

Human pro-urokinase (pro-UK) was cloned into plasmid pET32b and fused to the E. coli thioredoxin (trxA). When expressed in E. coli AD494(DE3), the fusion protein Trx-pro-UK accumulated as insoluble inclusion bodies and amounted to 35% of total cellular proteins. When co-expressed with molecular chaperones human protein disulfide isomerase (PDI) and E. coli GroESL, all the expressed products still existed in the form of insoluble inclusion bodies.

摘要

人尿激酶原(pro-UK)被克隆到质粒pET32b中,并与大肠杆菌硫氧还蛋白(trxA)融合。当在大肠杆菌AD494(DE3)中表达时,融合蛋白Trx-pro-UK以不溶性包涵体的形式积累,占细胞总蛋白的35%。当与人蛋白质二硫键异构酶(PDI)和大肠杆菌GroESL分子伴侣共表达时,所有表达产物仍以不溶性包涵体的形式存在。

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