A novel thrombolytic and anticoagulant serine protease from Polychaeta, Diopatra sugokai.

This study was aimed at assessing the fibrinolytic and anticoagulation features of a novel serine protease extracted and purified from Diopatra sugokai, a polychaeta that inhabits tidal flats. The purified serine protease was obtained through ammonium sulfate precipitation, affinity chromatography, and ion exchange chromatography. Its molecular size was identified via SDS-PAGE. To characterize its enzymatic activities, protease activity at various pH and temperatures, and in the presence of various inhibitors, was measured via azocasein assay. Its fibrinolytic activity and anticoagulant effect were assessed by fibrin zymography, fibrin plate assay, and fibrinogenolytic activity assays. The novel 38 kDa serine protease had strong indirect thrombolytic activity rather than direct activity over broad pH (4-10) and temperature (37°C-70°C) ranges. In addition, the novel serine protease exhibited anticoagulant activity by degrading the α-, β-, and γ- chains of fibrinogen. In addition, it did not produce cytotoxicity in endothelial cells. Therefore, this newly isolated serine protease is worthy of further investigation as a novel alkaline serine protease for thrombolytic therapy against brain ischemia. PMID: 29212289 [PubMed - as supplied by publisher]
Source: Journal of Microbiology and Biotechnology - Category: Biotechnology Authors: Tags: J Microbiol Biotechnol Source Type: research