ScholarLens Back to search
1998•IUBMB LifeRequires access

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

Ai‐Long Sun, Zichun Hua, Yao Ju, Yonghua Yang, Daqiang Yin

Open publisher page 8 citations

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.

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 8 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Inclusion bodies, Thioredoxin, Escherichia coli, Fusion protein, Protein disulfide-isomerase, Plasmid, Biochemistry, Recombinant DNA

Related papers

Related paper 1Related paper 2Related paper 3
Back to paper searchBrowse research topicsOriginal source
Fusion expression of human pro‐urokinase with E. coli thioredoxin — Research Paper | ScholarLens