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. 2022 Jul 19;2022:2748962. doi: 10.1155/2022/2748962

Figure 1.

Figure 1

Purification and characterization of BjussuMP-II. (a) Chromatographic profile of B. jararacussu venom using cation exchange chromatography. Fraction 4 was selected for presenting a relative molecular mass of 24 kDa in electrophoretic analysis on a 12.5% polyacrylamide gel. (b) Polyacrylamide gel electrophoresis (12.5%) of the fraction corresponding to the metalloprotease isolated from B. jararacussu venom (1) and of the purified metalloprotease BjussuMP-II, with an approximate molecular mass of 24 kDa (2). (c) Mass spectrum of BjussuMP-II in AXIMA TOF2. The spectrum measures the mass of the protein BjussuMP-II, at 23,423.40 Da. (d) Electrophoretic analysis of the fibrinogenolytic activity of B. jararacussu venom and BjussuMP-II at different incubation times, for 30 min (6), 1 h (7), 3 h (8), and 6 h (9). The negative control corresponds to fibrinogen (5).