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Identification of a new serine protease from polychaeta, Marphysa sanguinea, for its thrombolytic and anticoagulant activity

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Abstract

A serine protease was purified from Marphysa sanguinea through ammonium sulfate followed by ion exchange chromatography, and its N-terminal amino sequence was identified to be IVGGSEATPYQFPFQ. Fibrinolytic activity was depended on both direct fibrinolysis and indirect plasminogen-mediated cascade and had a consistent activity irrespective of pH. The serine protease could be confirmed to degrade α-, β-, and γ-chains of human fibrinogen through fibrinogenolytic assay and did not express significant cytotoxicity to endothelial cells. These imply the enzyme has anticoagulant as well as thrombolytic activity, not significantly impairing endothelial cells comprising brain blood brain barrier (BBB) tissue. Conclusively, the new serine protease is worthy of being a candidate to substitute tissue-Plasminogen Activator (t-PA) for acute ischemic reperfusion injury of brain.

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Authors and Affiliations

  1. Department of Biological Engineering, Inha University, Incheon, 22212, Korea

    Seung Ju Yeon, Kyou Hee Shim & Hwa Sung Shin

  2. Department of Oceanography, Inha University, Incheon, 22212, Korea

    Jae Sang Hong

  3. Korea Institute of Coastal Ecology, Inc., Ojeong-gu, Bucheon, 14449, Korea

    Jae Sang Hong

Authors
  1. Seung Ju Yeon
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  2. Kyou Hee Shim
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  4. Hwa Sung Shin
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Correspondence to Hwa Sung Shin.

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These authors contributed equally to this work.

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Yeon, S.J., Shim, K.H., Hong, J.S. et al. Identification of a new serine protease from polychaeta, Marphysa sanguinea, for its thrombolytic and anticoagulant activity. Korean J. Chem. Eng. 34, 781–786 (2017). https://doi.org/10.1007/s11814-016-0331-z

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  • DOI: https://doi.org/10.1007/s11814-016-0331-z

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