High level secretion of recombinant staphylokinase into periplasm of Escherichia coli
The staphylokinase (SAK) gene from Staphylococcus aureus NCTC10033 was inserted into an expression vector, pKK-ompA, having a tac promoter and an ompA signal sequence. Escherichia coli JM109 carrying the recombinant plasmid produced and secreted the recombinant SAK (rSAK) at 15ug/ml into periplasm and 5ug/ml to extracellular media, respectively. The rSAK was purified with 59% yield by simple procedures from the periplasm of E. coli. The aminoterminal sequence and human plasminogen activating activity of rSAK were coincided with the authentic SAK.
- Publisher
- Springer
- Issue Date
- 1998
- Language
- English
- Article Type
- Article
- Keywords
EXPRESSION; STREPTOKINASE; MECHANISM; CLONING; GENE
- Citation
BIOTECHNOLOGY LETTERS, v.20, no.2, pp.113 - 116
- ISSN
- 0141-5492
- Appears in Collection
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