Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195295
Type: Artigo de periódico
Title: Primary Structure Characterization Of Bothrops Jararacussu Snake Venom Lectin.
Author: de Carvalho, Daniela D
Marangoni, Sergio
Novello, José C
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.
Subject: Amino Acid Sequence
Animals
Bothrops
Crotalid Venoms
Cysteine Endopeptidases
Lectins
Molecular Sequence Data
Peptides
Protein Structure, Tertiary
Rats
Sequence Alignment
Sequence Analysis, Protein
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/11902666
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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