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In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai

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Academic year: 2019

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Fig. 1 SDS-PAGE profile and fibrinolytic activity of NnV. a We compared the fibrinolytic activity between jellyfish species
Fig. 3 The catalytic activity of NnV on several chromogenic substrates. a NnV was preincubated with different substrates [N-Succinyl-Ala-Ala-Ala- [N-Succinyl-Ala-Ala-Ala-ρNA (for elastase), Nα-Benzoyl-DL-Arg-[N-Succinyl-Ala-Ala-Ala-ρNA (for trypsin), N-(p-
Fig. 4 The catalytic activity of NnV was dependent on pH, temperature and metal ions. NnV (2 mg/mL) was incubated under different (a) pH (3, 4, 5, 6, 7, 8, 9, 10 and 11), (b) temperatures (4, 25, 37, 60 and 100 °C) and (c) metal ions (Ca 2+ , Co 2+ , Cu 2+
Fig. 5 The purification of serine protease from NnV. a Crude venom was dissolved in 10 mM Tris-HCl (pH 7.8) buffer and centrifuged for 30 min at 13000 × g

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