Characterization of a Bothrops alternatus metalloproteinase

GAY, CLAUDIA C.; .LEIVA, LAURA C.A.; ACOSTA, OFELIA C.; DEL CANTO, SERGIO; BISCOGLIO DE JIMÉNEZ BONINO, MIRTHA

Pinamar, Buenos Aires

Congreso; X PABMB Congress, SAIB XLI Annual Meeting, SAN XX Annual Meeting.; 2005

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular

Snake venoms metalloproteinases (SVMPs) play an important role in hemorrhage and disturbances of the hemostasis. Bothrops alternatus is the specie responsible for most of snakebites in north-eastern Argentina. In this work a metalloproteinase from Bothrops alternatus venom was isolated and its functional and structural aspects were studied to attempt a description of molecular features involved in its hemorrhagic activity. The enzyme (50 kDa) was digested in gel by trypsin and the peptide mixture submitted to MS (LCQ-DUO ESI-Ion Trap). Sequest analysis allowed identification of three fragments belonging to the carboxyl cysteine-rich domain of some members of this protein family apart from one fragment of the proteinase domain. The tryptic digest was also submitted to RPHPLC. Edman degradation of several fractions followed by sequence alignment was carried out. Studies indicated that the protein has a high degree of homology with jararhagin from Bothrops jararaca. Results, taken as a whole, lead to the conclusion that the enzyme belongs to the P-III type of SVMPs.