Citation

Naves de Souza DL, Gomes MSR, Ferreira FB, Rodrigues RS, Achê DC, Richardson M, Borges MH, Rodrigues VM. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2012; 161(2): 102-109.

Affiliation

Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia (UFU), Uberlândia, Minas Gerais, Brazil; Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), Belo Horizonte, Minas Gerais, Brazil.

Copyright

(Copyright © 2012, Elsevier Publishing)

DOI

10.1016/j.cbpb.2011.10.002

PMID

22008900

Abstract

Snake Venom Metalloproteinases (SVMPs) are the most abundant components present in Viperidae venom. They are important in the induction of systemic alterations and local tissue damage after envenomation. In the present study, a metalloproteinase named BpMPI was isolated from Bothropoides pauloensis snake venom and its biochemical and enzymatic characteristics were determined. BpMPI was purified in two chromatography steps on ion exchange CM-Sepharose Fast flow and Sephacryl S-300. This protease was homogeneous on SDS-PAGE and showed a single chain polypeptide of 20kDa under non reducing conditions. The partial amino acid sequence of the enzyme showed high similarity with other SVMPs enzymes from snake venoms. BpMPI showed proteolytic activity upon azocasein and bovine fibrinogen and was inhibited by EDTA, 1,10 phenanthroline and β-mercaptoethanol. Moreover, this enzyme showed stability at neutral and alkaline pH and it was inactivated at high temperatures. BpMPI was able to hydrolyze glandular and tissue kallikrein substrates, but was unable to act upon factor Xa and plasmin substrates. The enzyme did not induce local hemorrhage in the dorsal region of mice even at high doses. Taken together, our data showed that BpMP-I is in fact a fibrinogenolytic metalloproteinase and a non hemorrhagic enzyme.

Language: en