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

Fig. 1

From: Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Fig. 1

Isolation of Bordonein-L. Absorbance was monitored at 280 nm, at 25 °C, using a FPLC Äkta Purifier UPC-10 system. The dotted lines represent the concentration gradient. The vertical bars indicate the LAAO activity. a CdtV (1 g) was dispersed in 50 mL of 0.05 M sodium acetate buffer, pH 5.5 (buffer A) and the supernatant was fractionated on a CM-cellulose-52 column (1.0 × 40 cm) using a concentration gradient from 0 to 100 % of buffer B (1 M NaCl in buffer A). b The fraction CM5 was filtered on a HiPrep 16/60 Sephacryl S-100 HR column (1.6 × 60 cm) using 0.05 M sodium acetate buffer containing 0.15 M NaCl, pH 5.5. c Affinity chromatography of the CM5S2 fraction on HiTrap Heparin HP column (two 1-mL columns connected in series) using a concentration gradient from 0 to 100 % of buffer B. d Reversed-phase FPLC of H7 (bordonein-L) on a C4 column (0.46 × 25 cm, 5 μm particles) using a concentration gradient from 0 to 100 % of solution B (60 % acetonitrile in 0.1 % TFA)

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