Purification and functional characterization of a new metalloproteinase (BleucMP) from Bothrops leucurus snake venom

Autor: Marcelo Valle de Sousa, Elaine Nascimento Aquino, Mariana S. Castro, Mayara Ribeiro de Queiroz, Amélia Hamaguchi, Carla Cristine Neves Mamede, Maria Inês Homsi-Brandeburgo, Mário Sérgio Rocha Gomes, Fábio Luiz de Oliveira, Mirian Machado Mendes, Veridiana M. Rodrigues
Rok vydání: 2011
Předmět:
Zdroj: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology. 153:290-300
ISSN: 1532-0456
Popis: A fibrino(geno)lytic nonhemorrhagic metalloproteinase ( BleucMP ) was purified from Bothrops leucurus snake venom by two chromatographic steps procedure on DEAE-Sephadex A-25 followed by CM-Sepharose Fast Flow column. BleucMP represented 1.75% (w/w) of the crude venom and was homogeneous on SDS-PAGE. BleucMP analyzed by MALDI TOF/TOF, showed a molecular mass of 23,057.54 Da and when alkylated and reduced, the mass is 23,830.40 Da. Their peptides analyzed in MS (MALDI TOF\TOF) showed significant score when compared with those of other proteins by NCBI-BLAST2 alignment display. As regards their proteolytic activities, BleucMP efficiently acted on fibrinogen, fibrin, and was inhibited by EDTA and 1.10-phenanthroline. This enzyme was also able to decrease significantly the plasma fibrinogen level provoking blood incoagulability, however was devoid of hemorrhagic activity when tested in the mice skin and did not induce relevant biochemical, hematological and histopathological alterations in mice. The aspects addressed in this paper provide data on the effect of BleucMP in envenomation from B. leucurus snakes in order to better understand the effects caused by snake venom metalloproteinase.
Databáze: OpenAIRE