Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8333893 | International Journal of Biological Macromolecules | 2013 | 8 Pages |
Abstract
In the present work, we report the isolation and partial biochemical characterization of BpLec, a C-type lectin purified from Bothrops pauloensis venom by one chromatographic step on an affinity agarose column immobilized with d-galactose. This protein was homogeneous by SDS-PAGE under reducing and nonreducing conditions, and was shown to be a 33.6 kDa homodimer by MALDI TOF analysis. BpLec presented an isoeletric point of 5.36. Its partial sequence of 132 amino acids for each subunit, determined by Edman degradation, revealed high identity (between 86% and 95%) when aligned with sequences of other related proteins. BpLec was capable of agglutinating native dog and cat erythrocytes and this activity was inhibited by β-galactosides and EDTA. Its hemagglutinating activity was abolished at high temperatures and stable in any pH range. BpLec was effective in inhibiting Gram-positive but not Gram-negative bacteria. In addition, BpLec agglutinated promastigote forms of Leishmania (Leishmania) amazonensis.
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Authors
LetÃcia Eulálio Castanheira, Débora Cristina de Oliveira Nunes, Thomaz Monteiro Cardoso, Paula de Souza Santos, Luiz Ricardo Goulart, Renata Santos Rodrigues, Michael Richardson, Márcia Helena Borges, Kelly Aparecida Geraldo Yoneyama,