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dc.creatorGutiérrez, José María
dc.creatorRomero, Marjorie
dc.creatorDíaz Oreiro, Cecilia
dc.creatorBorkow, Gadi
dc.creatorOvadia, Michael
dc.date.accessioned2016-11-11T15:33:01Z
dc.date.available2016-11-11T15:33:01Z
dc.date.issued1995-01
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/10669/29235
dc.description.abstractA metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme has a mol. wt of 24,000 and contains few Cys and high numbers of Asp, Leu, Ser and Glu. BaP1 hydrolyzes casein, hide powder azure and fibrinogen, having an optimal pH of 8.0. It rapidly digests the A alpha-chain of fibrinogen and, later on, the B beta-chain, leaving the gamma-chain unaffected. Chelating agents (EDTA and 1,10-phenanthroline) inhibited proteolytic activity, whereas 2-mercaptoethanol and soybean trypsin inhibitor did not affect this activity. BaP1 has a weak hemorrhagic activity, with a minimum hemorrhagic dose of 20 micrograms; this activity was inhibited by EDTA and was abolished after incubation at 60 degrees C. In addition, BaP1 induces edema and a mild myotoxic effect, lacking coagulant, defibrinating and lethal effects.es_ES
dc.language.isoen_USes_ES
dc.sourceToxicon; Volumen 33, Número 1, 1995es_ES
dc.subjectAmino Acidses_ES
dc.subjectAnimalses_ES
dc.subjectBothropses_ES
dc.subjectCrotalid Venomses_ES
dc.subjectHemorrhagees_ES
dc.subjectMetalloendopeptidaseses_ES
dc.subjectMicees_ES
dc.subjectMolecular Weightes_ES
dc.subjectSnake venomes_ES
dc.titleIsolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/0041-0101(94)00138-X
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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