| Author | Silva, F. P. | |
| Author | Alexandre, G. M. C. | |
| Author | Ramos, C. H. I. | |
| Author | De Simone, Salvatore Giovanni | |
| Access date | 2019-04-09T16:12:01Z | |
| Available date | 2019-04-09T16:12:01Z | |
| Document date | 2008 | |
| Citation | SILVA JR., F. P. et al. On the quaternary structure of a C-type lectin from Bothrops jararacussu venom - BJ-32 (BjcuL). Toxicon, v. 52, p. 944-953, 2008. | pt_BR |
| ISSN | 0041-0101 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/32424 | |
| Language | eng | pt_BR |
| Publisher | Elsevier | pt_BR |
| Rights | restricted access | |
| Subject in Portuguese | Estrutura quaternária | pt_BR |
| Subject in Portuguese | Oligomerização | pt_BR |
| Subject in Portuguese | Estrutura de solução | pt_BR |
| Subject in Portuguese | Lectina do veneno da serpente | pt_BR |
| Title | On the quaternary structure of a C-type lectin from Bothrops jararacussu venom--BJ-32 (BjcuL) | pt_BR |
| Type | Article | |
| DOI | 10.1016/j.toxicon.2008.10.014 | |
| Abstract | BJ-32 (also known as BjcuL) is a C-type lectin from the venom of Bothrops jararacussu with specificity for beta-galactosides and a remarkable ability to agglutinate several species of trypanosomatids. Our objective was to study the oligomerization state of native BJ-32 by using different biophysical and computational methods. Small-angle X-ray light scattering (SAXS) experiments disclosed a compact, globular protein with a radius of gyration of 36.72+/-0.04A and molecular weight calculated as 147.5+/-2.0kDa. From analytical ultracentrifugation analysis, it was determined that the BJ-32 sedimentation profile fits nicely to a decamer model. The analysis of the intrinsic emitted fluorescence spectra for BJ-32 solutions indicated that association of subunits in the decamer is accompanied by changes in the environment of Tryptophan residues. Both ab initio and comparative models of BJ-32 supported the resemblance of the decamer in the crystallographic structure from a close homologue, the rattlesnake venom lectin (RSL) from Crotalus atrox. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteínas e Peptídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteínas e Peptídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade de Campinas. Instituto de Química. Campinas, SP, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteínas e Peptídeos. Rio de Janeiro, RJ, Brasil / Universidade Federal Fluminense. Instituto de Biologia. Departamento de Biologia Celular e Molecular. Niterói, RJ, Brasil. | pt_BR |
| Subject | Oligomerization | pt_BR |
| Subject | Quaternary structure | pt_BR |
| Subject | Solution structure | pt_BR |
| Subject | Snake venom lectin | pt_BR |
| e-ISSN | 1879-3150 | |
| Embargo date | 2022-01-01 | |
