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 β-galactoside binding lectin family.
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de Carvalho, D.D., Marangoni, S. & Novello, J.C. Primary Structure Characterization of Bothrops jararacussu Snake Venom Lectin. J Protein Chem 21, 43–50 (2002). https://doi.org/10.1023/A:1014131115951
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DOI: https://doi.org/10.1023/A:1014131115951