An efficient system for production of recombinant urokinase-type plasminogen activator

Protein Expression and Purification
W TangJ N Liu

Abstract

A system was developed to produce recombinant urokinase-type plasminogen activator in Escherichia coli. The urokinase-type plasminogen activator was produced with a 6 x His-tag at the C-terminus which was shown to have the same activity, after refolding, as the wild-type protein. Purification of the recombinant protein to homogeneity (95%) was possible by one-step affinity chromatography under denaturing conditions. As a result, proteolysis by bacterial proteases during purification was avoided. A higher refolding efficiency (40%) and a higher total recovery yield (25%) of the recombinant protein were obtained by this method.

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Citations

Dec 6, 2011·Microbial Cell Factories·Neus Ferrer-MirallesEsther Vazquez
Feb 6, 2009·Biotechnology Progress·Shilpa S KhapardeAsok Mukhopadhyay
Feb 15, 2011·Biotechnology Letters·Wen-Hui K Kuo, Howard A Chase
Mar 21, 2001·Biotechnology & Genetic Engineering Reviews·L M BabéB F Schmidt
Mar 31, 2021·Biomacromolecules·Keiichi YoshimatsuKenneth J Shea
Mar 28, 2021·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Beatrice SakhelPaul Adams
May 27, 2021·Biochemistry and Biophysics Reports·Daniel R TurkewitzStella M Valenzuela
Mar 1, 2006·Protein Expression and Purification·Jian LinWenyan Wu
Jan 24, 2006·Protein Expression and Purification·José ArnauJohn Pedersen
Jul 11, 2006·Biotechnology Advances·Pradip K RoychoudhuryAshok Kumar
Aug 15, 2006·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Mouna Amor-MahjoubMoncef Ladjimi

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