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 a...

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Veröffentlicht in:Biotechnology letters 1998-02, Vol.20 (2), p.113-116
Hauptverfasser: Lee, Sang Jun, Kim, Il Chul, Kim, Dong Min, Bae, Kwang Hee, Byun, Si Myung
Format: Artikel
Sprache:eng
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Zusammenfassung: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.[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005359920522