Resumo

LAZO, Fanny; MALAGA, Orestes; YARLEQUE, Armando  e  SEVERINO, Ruperto. Some biochemical properties of a L- amino acid oxidase isolated from Bothrops atrox snake venom. Rev. Soc. Quím. Perú [online]. 2007, vol.73, n.3, pp.131-141. ISSN 1810-634X.

A L-amino acid oxidase enzyme was purified and characterized from Bothrops atrox snake venom by two steps. It used a Sephadex G-100 coulmn and ion exchange on CM Sephadex C-50 at pH 6. The p grade was 12,14 folds with a specific activity of 4,13 U/mg. The enzyme with a molecular weight of 127, 879 Daltons as determined by gel filtration, is a noncovalent dimmer consisting of two subunits with a molecular weight each of 63, 128 Daltons as determined by SDS-PAGE, with at least one intrachain disulfide bond that is important for its activity. The enzyme exhibited a opt pH 8,3 using L-leucine as substrate. It is an acid glicoprotein containing 17% carbohydrates, being thermoestable till 55,labil to alkaline pH and susceptible to presence of Zn2+ (6mM). Immunodiffusion and immunoelectrophoresis assays, using polivalente botropic antivenom, showed that LAO is antigenic protein.

Palavras-chave : L-amino acid oxidase; snake; enzyme; Bothrops atrox; venom.

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