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Fig. 3 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 3

From: Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom

Fig. 3

Enzymatic activity of Lmr-MP upon inhibitors and different ions. a Azocaseinolytic activity of Lmr-MP (10 μg/100 μL): in the absence (control) or presence of 10 mM different inhibitors (EDTA, IAA, PEPS and PMSF). b in the presence of 10 mM different ions (CoCl2, LiCl, MgCl2, KCl, ZnCl2, NiSO4, CuCl2, CaCl2, MnCl2, AlCl3, BaCl2 and NaCl). c in the presence of ZnCl2 at different concentrations (2.5, 5.0, 7.5 and 10 mM). The reactions were performed at 37 °C. The residual activity was determined based on control activity: Residual activity = 100 x [(Sample activity)/ (Control activity)]. *p < 0.05, ** p < 0.01 and *** p < 0.0001 compared to the controls (one-way ANOVA, followed by Dunnett’s test). Data (n = 3) are presented as mean ± SD

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