Fibrinolytic Activity of a Novel Serine Protease from the Hemolymph of a Polychaeta, Periserrula leucophryna
- Authors
- Kool, Kwang Bon; Suh, Hyung Joo; Ra, Kyung Soo; Kim, Yeon Hyang; Joo, Han-Seung; Choi, Jang Won
- Issue Date
- 4월-2010
- Publisher
- KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
- Keywords
- fibrinolytic activity; Periserrula leucophryna; plasmin-like activity; polychaeta; serine protease
- Citation
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.53, no.2, pp.149 - 157
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
- Volume
- 53
- Number
- 2
- Start Page
- 149
- End Page
- 157
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/116744
- DOI
- 10.3839/jksabc.2010.025
- ISSN
- 1738-2203
- Abstract
- We purified and characterized a novel protease with fibrinolytic activity from the hemolymph of a polychaeta, Periserrula leucophryna. The enzyme was isolated by chromatographic methods using Phenyl-Sepharose and Benzamidine-Sepharose. SDS-PAGE and gel filtration revealed a single polypeptide chain with a molecular weight of 30 kDa. The N-terminal sequence was determined to be IVGGQNARQGEFPWQV. The purified enzyme preferentially cleaved the synthetic substrates that had Lys (rather than Arg) at the P-1 position and did not efficiently cleave substrates with non-polar amino acids. Among chromogenic protease substrates, the substrate that was most susceptible to hydrolysis by Periserrula leucophryna fibrinolytic protease (PLFP) was Val-Leu-Lys-pNA (substrate for plasmin). The inhibition profile revealed the protease belongs to a family of serine proteases and has plasmin-like activity that is strongly inhibited by alpha 2-antiplasmin. The purified PLFP was able to dissolve the artificial fibrin, and its fibrinolytic behavior is similar to that of plasmin. In conclusion, PLFP is a novel protease and has potential for practical applications in thrombolytic therapy.
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Collections - College of Health Sciences > School of Biosystems and Biomedical Sciences > 1. Journal Articles
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