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Abstract Objective Using the recombinant staphylokinase there is a lack of ten amino acids in the N end to construct engineering bacterium expressing soluble protein. Research the content of recombinant staphylokinase gained at different induced conditions and the way of purification. Methods The aim protein of recombinant staphylokinase induced using the activation and cultivation of bacteria and its content measured with SDS-PAGE. The protein was purified with chromatography. Result The content of induced recombinant staphylokinase was about 50% of total protein. After purification, the rate of recollected aim protein was 60% and its purity was over 99%. Conclusion The engineering bacteria of induced aim protein of recombinant staphylokinase were successfully constructed. The high expression and purified protein was acquired.
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Received: 22 September 2005
Published: 25 May 2006
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