Citation

Gomes MSR, de Queiroz MR, Mamede CC, Mendes MM, Hamaguchi A, Homsi-Brandeburgo MI, Sousa MV, Aquino EN, Castro MS, de Oliveira F, Rodrigues VM. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2011; 153(3): 290-300.

Affiliation

Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia(UFU), 38400-902 Uberlândia-MG, Brazil; Departamento de Química e Exatas, Universidade Estadual do Sudoeste da Bahia(UESB), 45506-210 Jequié-BA, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), 31270-901, Belo Horizonte-MG, Brazil.

Copyright

(Copyright © 2011, Elsevier Publishing)

DOI

10.1016/j.cbpc.2010.11.008

PMID

21130897

Abstract

A fibrino(geno)lytic nonhemorrhagic metalloproteinase (BleucMP) was purified from Bothrops leucurus snake venom by two chromatographic step 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 23057.54Da and when alkylated and reduced, the mass is 23830.40Da. Their peptides analyzed in MS (MALDI TOFTOF) 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 alterarions in mice. The aspects addressed in this paper provide data on the effect of BleucMP in envenomation from Bothrops leucurus snakes in order to better understand the effects caused by snake venom metalloproteinase.

Language: en