Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/196598
Type: Artigo de periódico
Title: Purification And Characterization Of A Hemorrhagic Metalloproteinase From Bothrops Lanceolatus (fer-de-lance) Snake Venom.
Author: Stroka, Alessandra
Donato, José L
Bon, Cassian
Hyslop, Stephen
de Araújo, Albetiza Lôbo
Abstract: Bothrops snake venoms contain metalloproteinases that contribute to the local effects seen after envenoming. In this work, a hemorrhagic metalloproteinase (BlaH1) was purified from the venom of the snake Bothrops lanceolatus by a combination of gel filtration, affinity (metal chelating) and hydrophobic interaction chromatographies. The hemorrhagin was homogeneous by SDS-PAGE and had a molecular mass of 28 kDa that was unaltered by treatment with beta-mercaptoethanol. BlaH1 gave a single band in immunoelectrophoresis and immunoblotting using commercial bothropic antivenom. BlaH1 had hemorrhagic, caseinolytic, fibrinogenolytic, collagenolytic and elastinolytic activities, but no phospholipase A(2) activity. The hemorrhagic and caseinolytic activities were inhibited by EDTA, indicating that they were metal ion-dependent. In contrast, aprotinin, benzamidine and PMSF did not affect these activities. The caseinolytic activity of BlaH1 had a pH optimum of 8.0 and was stable in solution at up to 40 degrees C; activity was completely lost at > or =70 degrees C. The hemorrhagic activity was neutralized by commercial bothropic antivenom. These properties suggest that this new hemorrhagin belongs to class P-I snake venom metalloproteinases.
Subject: Animals
Aprotinin
Benzamidines
Bothrops
Caseins
Chromatography, Affinity
Chromatography, Gel
Collagenases
Crotalid Venoms
Edetic Acid
Electrophoresis, Polyacrylamide Gel
Endopeptidases
Esterases
Fibrinogen
Immunoblotting
Male
Metalloendopeptidases
Phospholipases A
Rats
Rats, Wistar
Temperature
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2004.11.010
Address: http://www.ncbi.nlm.nih.gov/pubmed/15733562
Date Issue: 2005
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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