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In relation to this article, we declare that there is no conflict of interest.
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Received September 27, 2016
Accepted November 20, 2016
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Identification of a new serine protease from polychaeta, Marphysa sanguinea, for its thrombolytic and anticoagulant activity

1Department of Biological Engineering, Inha University, Incheon 22212, Korea 2Department of Oceanography, Inha University, Incheon 22212, Korea 3Korea Institute of Coastal Ecology, Inc., Ojeong-gu, Bucheon 14449, Korea
hsshin@inha.ac.kr
Korean Journal of Chemical Engineering, March 2017, 34(3), 781-786(6), 10.1007/s11814-016-0331-z
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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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