title: Primary structure characterization of Bothrops jararacussu snake venom lectin.
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.
authors.affiliation: Universidade Estadual de Campinas (UNICAMP), Instituto de Biologia, Departamento de Bioquímica, LAQUIP, Campinas-SP, Brazil.
authors.forename: Daniela D
authors.initials: DD
authors.lastname: de Carvalho
authors.forename: Sergio
authors.initials: S
authors.lastname: Marangoni
authors.forename: José C
authors.initials: JC
authors.lastname: Novello
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry* / Q000235:genetics; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis; D017434:Protein Structure, Tertiary; D051381:Rats; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein
chemical_list: D003435:Crotalid Venoms; D037102:Lectins; D010455:Peptides; D003546:Cysteine Endopeptidases; C019913:clostripain