Abstract
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 amino-terminal sequence and human plasminogen activating activity of rSAK were coincided with the authentic SAK.
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Lee, S.J., Kim, I.C., Kim, D.M. et al. High level secretion of recombinant staphylokinase into periplasm of Escherichia coli. Biotechnology Letters 20, 113–116 (1998). https://doi.org/10.1023/A:1005359920522
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DOI: https://doi.org/10.1023/A:1005359920522