BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
---|---|
Data(s) |
19/10/2012
19/10/2012
2009
|
Resumo |
In this work, a new weakly hemorrhagic metalloproteinase (BthMP) was purified from Bothrops moojeni snake venom. This enzyme was homogeneous by native and SDS-PAGE. It showed a polypeptide chain of 23.5 kDa, pI=7.1, and N-terminal blocked. BthMP is comprised of high proteolytic activity on casein, fibrin and bovine fibrinogen, with no coagulating, esterase or phospholipase A(2) activities; it was inhibited by EDTA, EGTA and 1,10-phenanthroline and maintained its activity on pH from 7.0 to 9.0 and temperature from 5-40 degrees C. Assays with metal ions showed that Ca(2+) is an activator, whereas Zn(2+) and Hg(2+) inhibited about 50 and 80% of its activity, respectively. The edema evidenced the important role of the toxin in the inflammatory activity of the venom. BthMP also caused unclotting, and provoked histological alterations in the gastrocnemius muscle of mice inducing hemorrhage, necrosis and leukocytic infiltrate. The molecular mass and the inhibition assays suggest that the metal loproteinase BthMP belongs to class P-I of SVMPs. (c) 2008 Elsevier Ltd. All rights reserved. |
Identificador |
TOXICON, v.53, n.1, p.24-32, 2009 0041-0101 http://producao.usp.br/handle/BDPI/20244 10.1016/j.toxicon.2008.10.007 |
Idioma(s) |
eng |
Publicador |
PERGAMON-ELSEVIER SCIENCE LTD |
Relação |
Toxicon |
Direitos |
restrictedAccess Copyright PERGAMON-ELSEVIER SCIENCE LTD |
Palavras-Chave | #Bothrops moojeni #Metalloproteinase #Snake venom #P-III METALLOPROTEINASE #BIOCHEMICAL-CHARACTERIZATION #FUNCTIONAL-CHARACTERIZATION #BOTHROPS-MOOJENI-(CAISSACA) VENOM #POLYACRYLAMIDE GELS #BASIC PROTEINASES #JARARHAGIN #LEUCURUS #PURIFICATION #JARARACA #Pharmacology & Pharmacy #Toxicology |
Tipo |
article original article publishedVersion |