Primary structure characterization of Bothrops jararacussu snake venom lectin.
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.
de Carvalho
Daniela D
DD
Universidade Estadual de Campinas (UNICAMP), Instituto de Biologia, Departamento de Bioquímica, LAQUIP, Campinas-SP, Brazil.
Marangoni
Sergio
S
Novello
José C
JC
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
D003435:Crotalid Venoms; D037102:Lectins; D010455:Peptides; D003546:Cysteine Endopeptidases; C019913:clostripain