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Fig. 4 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 4

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

Fig. 4

Proteolytic activity of the fraction LmS-6. a upon 0.4 mM chromogenic substrates (Chromogenix®) for plasma kallikrein (S-2302), plasmin and plasminogen activated by streptokinase (S-2251) and Factor Xa (S-2222). ***p < 0.0001 compared among the tested substrates. b in the presence of different solutions. LmS-6 fraction (5 μg) was incubated with 5 and 50 mM AMBIC, pH 7.8; 0.1% TFA + 50% ACN; PBS, pH 7.4; 50 mM NaOAc, pH 4; 50 mM NH4OAc, pH 4.5 and 50 mM Tris-HCl, pH 8.0 at 37 °C for 90 min. Each point represents the mean ± SD (n = 3), *p < 0.05, ** p < 0.01 and *** p < 0.0001 compared to the negative control. The ## symbol represent the significant values when compared to PBS. c pH-profile of LmS-6 fraction at different pHs (4.5–9.0). Each point represents the mean ± SD (n = 3), *p < 0.05, ** p < 0.01 and *** p < 0.0001 compared to the controls (one-way ANOVA, followed by Dunnett’s test). NC is negative control and PC positive control

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