Resumo

GONZALEZ, Édgar et al. Purification and biochemical characterization of a spreading factor from the venom of snake Bothrops atrox (Jergon). Rev. Soc. Quím. Perú [online]. 2013, vol.79, n.1, pp.3-12. ISSN 1810-634X.

A protein of high molecular weight was purified from the venom of Bothrops atrox Peruvian snake, using DEAE Sephadex A-50 anion exchange chromatography and Sephadex G-50 gel molecular filtration, with 0,05M ammonium acetate, pH 5.0. It showed hyaluronidase activity, and was obtained until homogeneous state with a 145-fold, 72% of yield and a 0.5% of recovery of active protein. The enzyme showed a molecular weight of 110 kDa by SDS- PAGE under reducing and non reducing conditions. The stability assays indicated that hyaluronidase lost 60% of its activity after 150 hours at pH 5.0 and it was quickly inactivated by heat treatment above 40 ºC. The optimum pH was 6.0 using hyaluronic acid and some inhibitors such as TLCK, iodoacetate and dexamethasone (5 mM), caused 60, 40 and 75% of inactivation, respectively. On the other hand, this enzyme is capable to increase hemolysis into agar plates. Furthermore, treatment of the enzyme with human blood-serum, as well as lachesic and bothropic commercial antivenoms produced a strong inhibition; also, IgY experimental antivenom revealed high inhibition of this enzyme.

Palavras-chave : Venom; snake; Amazon; hyaluronic acid; enzyme; antivenom.

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