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Fig. 7 | Parasites & Vectors

Fig. 7

From: Molecular characterization and functional analysis of the Schistosoma mekongi Ca2+-dependent cysteine protease (calpain)

Fig. 7

Proteolytic activity of rSmeCalp1. a rSmeCalp1 elicited proteolytic activity to hydrolyze the calpain fluorogenic substrate (N-succinyl-Leu-Leu-Val-Try-7-AMC), and irrelevant (rmDHFR) and negative controls could not be detected. b Proteolytic activity of rSmeCalp1 was inhibited by calpain inhibitors (MDL and E64c), broad cysteine protease inhibitor (E64) and metal chelating agent (EDTA) but not by other protease class inhibitors (PMSF, Peps A and 1,10-Phen). Statistical analysis was performed using Student’s t-test. **P < 0.01. c Proteolytic activity of rSmeCalp1 was dependent on concentration of Ca2+. d A wide pH range for proteolytic activity of rSmeCalp1 was observed (6.5–9.5) with an optimum pH at 8.5. Data are presented as means ± standard deviations. The experiments were performed in triplicate and repeated three times

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