TY  - JOUR
PY  - 2011//
TI  - Purification and functional characterization of a new metalloproteinase (BleucMP) from Bothrops leucurus snake venom
JO  - Comparative Biochemistry and Physiology, C: Toxicology and Pharmacology
A1  - Gomes, Mário Sérgio R.
A1  - de Queiroz, Mayara R.
A1  - Mamede, Carla C. N.
A1  - Mendes, Mirian M.
A1  - Hamaguchi, Amélia
A1  - Homsi-Brandeburgo, Maria I.
A1  - Sousa, Marcelo V.
A1  - Aquino, Elaine Nascimento
A1  - Castro, Mariana S.
A1  - de Oliveira, Fábio
A1  - Rodrigues, Veridiana M.
SP  - 290
EP  - 300
VL  - 153
IS  - 3
N2  - 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.<p />  <p>Language: en</p>
LA  - en
SN  - 1532-0456
UR  - http://dx.doi.org/10.1016/j.cbpc.2010.11.008
ID  - ref1
ER  -