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• W2040697934 abstract "A non-hemorrhagic, chymotrypsin-like serine protease, UFEII, was purified from the marine echiuroid worm, Urechis unicinctus, after a combination of chromatography steps. UFEII was monomeric, with an apparent molecular weight of 26.7 kDa via SDS-PAGE. The isoelectric point of UFEII was 4.03, and the maximum activity of the enzyme was observed at 50 °C and pH 8.0. According to fibrin plate assays, UFEII could not only directly degrade fibrin and fibrinogen but also activate plasminogen. Further, UFEII preferentially hydrolyzed the fibrinogen γ-chain, followed by the Bβ-chains and Aα-chains. Moreover, ufeII, full length of the gene encoding UFEII, was obtained by RT-PCR, degenerated PCR, and nested PCR. The ufeII was determined to be a 906-bp cDNA containing an open reading frame of 795 bp encoding a putative protein of 264 amino acids with a predicted molecular weight of 27.03 kDa. Besides, UFEII exhibited no hemorrhagic effect. Overall, U. unicinctus may represent a potential source of new therapeutic agents in thrombolytic therapy." @default.
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• W2040697934 date "2013-04-04" @default.
• W2040697934 modified "2023-10-06" @default.
• W2040697934 title "Purification and Characterization of a New Serine Protease with Fibrinolytic Activity from the Marine Invertebrate, Urechis unicinctus" @default.
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• W2040697934 doi "https://doi.org/10.1007/s12010-013-0168-4" @default.
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