Resumo

PALOMINO, Mercedes et al. Purification of a lectin type c from the venom of Lachesis muta peruvian snake. Rev. Soc. Quím. Perú [online]. 2012, vol.78, n.3, pp.161-169. ISSN 1810-634X.

A lectin type C was purified and researching its biochemical properties from the venom of Lachesis muta Peruvian snake. Purification was performed through a unic chromatographic step using a DEAE-Sephadex A-50 column, equilibrated with 0,1 M ammonium acetate pH 5 buffer. A lectin was recognized for its capacity in vitro to agglutinating human red cells. This protein was purified 3,6 folds and it represents 3,5 % of the total protein into the venom. It had 27,5 kDa and 14,3 kDa of molecular weight in non reduction and reduction conditions, respectively, using a PAGE-SDS analysis. It was strongly inhibited by the lactose (1,56 mM) followed by galactose, arabinose, sacarose and glucose. While maltose, mannose and fructose were not inhibitors. Hemagglutinating activity was inhibited by EDTA, DTT and ME too using different concentrations. However inhibition produced by EDTA (0,125-0,5 mM) was abolished by Ca⁺², Mg⁺² and Mn⁺² ions. These results showed that this purified protein is a lectin type C, with a potent hemagglutinin activity.

Palavras-chave : Hemagglutinins snake; venom; Lachesis muta.

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