Expression of a deleted variant of human plasminogen in Escherichia coli
A recombinant plasmid carrying a modified gene of human plasminogen (mini-plasminogen), lacking four kringle domains and an amino terminal fragment, and containing an additional oligopeptide of six N-terminal histidine residues has been constructed. The plasmid was used for transformation of E. coli...
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Veröffentlicht in: | Applied biochemistry and microbiology 2010-12, Vol.46 (8), p.776-780 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A recombinant plasmid carrying a modified gene of human plasminogen (mini-plasminogen), lacking four kringle domains and an amino terminal fragment, and containing an additional oligopeptide of six N-terminal histidine residues has been constructed. The plasmid was used for transformation of E. coli JM 109 cells to obtain a strain producing a recombinant modified human plasminogen. The target protein is superexpressed in a form of inclusion bodies and is composed of more than 50% insoluble protein. The renaturated and chromatographically purified protein exhibits amidolytic activity specific for plasminogen proenzyme in a fibrinolytic system. |
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ISSN: | 0003-6838 1608-3024 |
DOI: | 10.1134/S0003683810080077 |