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Enhanced expression of an antibody-targeted plasminogen activator in Escherichia coli by fusion to decorsin

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Abstract

To improve the thrombolytic specificity of plasminogen activators, an antibody-targeted plasminogen activator was constructed consisting of a single-chain variable fragment of a monoclonal antibody SZ-51 raised specifically against human P-selectins on activated platelets and a low molecular weight single-chain urokinase. After fusion to the 3′ end of the gene coding for decorsin, originally isolated from the leechMacrobdella decora, expression of the antibody-targeted plasminogen activator gene in E. coli strain Rosetta (DE3) pLysS was greatly enhanced.

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Authors and Affiliations

  1. National Key Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, 100871, P.R. China

    Ming Yu, Meimin Yu & Binggen Ru

Authors
  1. Ming Yu
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  2. Meimin Yu
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  3. Binggen Ru
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Yu, M., Yu, M. & Ru, B. Enhanced expression of an antibody-targeted plasminogen activator in Escherichia coli by fusion to decorsin. Biotechnology Letters 26, 717–721 (2004). https://doi.org/10.1023/B:BILE.0000024095.83712.5e

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  • DOI: https://doi.org/10.1023/B:BILE.0000024095.83712.5e

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