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| Elífio-Esposito,S. L.; Hess,P. L.; Moreno,A. N.; Lopes-Ferreira,M.; Ricart,C. A. O.; Souza,M. V.; Hasselman-Zielinski,F.; Becker,J. A.; Pereira,L. F.. |
| Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Venoms; Fibronectins; Vitronectin; Snakes; Intravital microscopy; Leukocytes. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009 |
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