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Primary structure characterization of Bothrops jararacussu snake venom lectin
Daniela D de Carvalho1, Sergio Marangoni, José C Novello
1Universidade Estadual de Campinas (UNICAMP), Instituto de Biologia, Departamento de Bioquímica, LAQUIP, Campinas-SP, Brazil.
Abstract:
The complete amino acid sequence of the lectin from Bothrops jararacussu snake venom (BJcuL) is reported. The sequence was determined by Edman degradation and amino acid analysis of the S-carboxymethylated BJcuL derivative (RC-BJcuL) and from its peptides originated from enzymatic digestion. The sequence of amino acid residues showed that this lectin displays the invariant amino acid residues characterized in C-type lectins. Amino acids analysis revealed a high content of acidic amino acids and leucine. These findings suggest that BJcuL, like other snake venom lectins, possesses structural similarities to the carbohydrate recognition domain (CRD) of calcium-dependent animal lectins belonging to the C-type beta-galactoside binding lectin family.