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Fig. 1 | Journal of Venomous Animals and Toxins including Tropical Diseases

Fig. 1

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

Fig. 1

Chromatographic profiles of metalloprotease from L. m. rhombeata venom. a Fractionation of Lachesis muta rhombeata venom by molecular exclusion chromatography on a HiPrep Sephacryl® S-100 HR column (1.6 × 60 cm) using 0.05 M sodium acetate buffer with 0.15 M NaCl, pH 6.0. L. m. rhombeata venom (23 mg) was dispersed in 500 μL of buffer. Flow rate: 0.5 mL/min; fractions collected: 1.5 mL/tube. b Fractionation of LmS-6 on the ion exchange column HiTrap™ IEX SP XL (0.7 × 2.5 cm, 1 mL). The sample dispersed in buffer A (0.05 M MES - 2-(N-morpholino) ethanesulfonic acid, pH 6.0) was applied on the column and eluted using a concentration gradient from 0 to 1.0 M NaCl in the same buffer. Insert SDS-PAGE (13.5%) under reducing conditions. Lanes 1: molecular mass standard (Sigma cat. M0671); 2: molecular mass standard (GE Healthcare 17–0615-01); 3: L. m. rhombeata venom; 4: Fraction LmrS-6 from molecular exclusion fractionation; 5 and 6: Lmr-MP

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