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pubmed-article:9425632pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:9425632pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:9425632pubmed:year1997lld:pubmed
pubmed-article:9425632pubmed:articleTitleAn efficient system for production of recombinant urokinase-type plasminogen activator.lld:pubmed
pubmed-article:9425632pubmed:affiliationVascular Research Laboratory, Beth Israel-Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.lld:pubmed
pubmed-article:9425632pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9425632pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:9425632pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed