dc.creatorde Carvalho, Daniela D
dc.creatorMarangoni, Sergio
dc.creatorNovello, José C
dc.date2002-Jan
dc.date2015-11-27T12:49:34Z
dc.date2015-11-27T12:49:34Z
dc.date.accessioned2018-03-29T00:57:05Z
dc.date.available2018-03-29T00:57:05Z
dc.identifierJournal Of Protein Chemistry. v. 21, n. 1, p. 43-50, 2002-Jan.
dc.identifier0277-8033
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11902666
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195295
dc.identifier11902666
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295528
dc.descriptionThe 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.
dc.description21
dc.description43-50
dc.languageeng
dc.relationJournal Of Protein Chemistry
dc.relationJ. Protein Chem.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBothrops
dc.subjectCrotalid Venoms
dc.subjectCysteine Endopeptidases
dc.subjectLectins
dc.subjectMolecular Sequence Data
dc.subjectPeptides
dc.subjectProtein Structure, Tertiary
dc.subjectRats
dc.subjectSequence Alignment
dc.subjectSequence Analysis, Protein
dc.titlePrimary Structure Characterization Of Bothrops Jararacussu Snake Venom Lectin.
dc.typeArtículos de revistas


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