Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae)
Descripción del Articulo
A myotoxin from Bothrops atrox snake venom was purified by cationic exchange on CM-Sephadex C-50 with 0,05M ammonium acetate pH 7. The myotoxin is a basic protein and by gel filtration and PAGE-SDS was demonstrated that protein has a molecular weight of 27 kDa and two polipeptides chain of 14 kDa ea...
Autores: | , , |
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Formato: | artículo |
Fecha de Publicación: | 2004 |
Institución: | Universidad Nacional Mayor de San Marcos |
Repositorio: | Revistas - Universidad Nacional Mayor de San Marcos |
Lenguaje: | español |
OAI Identifier: | oai:ojs.csi.unmsm:article/2436 |
Enlace del recurso: | https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/2436 |
Nivel de acceso: | acceso abierto |
Materia: | miotoxina Bothrops atrox veneno de serpiente mionecrosis myotoxin snake venom myonecrosis |
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Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae)Aislamiento y caracterización parcial de una miotoxina del veneno de la serpiente Bothrops atrox (Ophidia: Viperidae)Huatuco, SergioEscobar, EnriqueYarlequé, ArmandomiotoxinaBothrops atroxveneno de serpientemionecrosismyotoxinBothrops atroxsnake venommyonecrosisA myotoxin from Bothrops atrox snake venom was purified by cationic exchange on CM-Sephadex C-50 with 0,05M ammonium acetate pH 7. The myotoxin is a basic protein and by gel filtration and PAGE-SDS was demonstrated that protein has a molecular weight of 27 kDa and two polipeptides chain of 14 kDa each one. The inoculation of myotoxin in gastrocnemius muscle of white mice produce liberation of creatin kinase as well as myonecrosis. The myotoxin has phospholipasic, anticoagulant and edematic activity, but not hemolytic activity.Se ha purificado una miotoxina del veneno de la serpiente Bothrops atrox, empleando una columna de intercambio catiónico de CM-Sephadex C-50 equilibrada con buffer acetato de amonio 0,05M a pH 7. La miotoxina es una proteína básica, y por cromatografía de filtración y PAGE-SDS se ha determinado que tiene un peso molecular de 27 kDa, estando formada por dos cadenas polipeptídicas de 14 kDa cada una. La inoculación de la miotoxina en el músculo gastrocnemius de ratones albinos produce la liberación de creatina kinasa así como la necrosis del tejido. La miotoxina tiene actividad de fosfolipasa, anticoagulante y edemática, pero no hemolítica.Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas2004-07-15info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/243610.15381/rpb.v11i1.2436Revista Peruana de Biología; Vol. 11 Núm. 1 (2004); 79-86Revista Peruana de Biología; Vol. 11 No. 1 (2004); 79-861727-99331561-0837reponame:Revistas - Universidad Nacional Mayor de San Marcosinstname:Universidad Nacional Mayor de San Marcosinstacron:UNMSMspahttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/2436/2134Derechos de autor 2004 Sergio Huatuco, Enrique Escobar, Armando Yarlequéhttps://creativecommons.org/licenses/by-nc-sa/4.0info:eu-repo/semantics/openAccessoai:ojs.csi.unmsm:article/24362020-05-25T11:29:34Z |
dc.title.none.fl_str_mv |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) Aislamiento y caracterización parcial de una miotoxina del veneno de la serpiente Bothrops atrox (Ophidia: Viperidae) |
title |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
spellingShingle |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) Huatuco, Sergio miotoxina Bothrops atrox veneno de serpiente mionecrosis myotoxin Bothrops atrox snake venom myonecrosis |
title_short |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
title_full |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
title_fullStr |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
title_full_unstemmed |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
title_sort |
Isolation and partial characterization of a myotoxin from Bothrops atrox snake venom (Ophidia: Viperidae) |
dc.creator.none.fl_str_mv |
Huatuco, Sergio Escobar, Enrique Yarlequé, Armando |
author |
Huatuco, Sergio |
author_facet |
Huatuco, Sergio Escobar, Enrique Yarlequé, Armando |
author_role |
author |
author2 |
Escobar, Enrique Yarlequé, Armando |
author2_role |
author author |
dc.subject.none.fl_str_mv |
miotoxina Bothrops atrox veneno de serpiente mionecrosis myotoxin Bothrops atrox snake venom myonecrosis |
topic |
miotoxina Bothrops atrox veneno de serpiente mionecrosis myotoxin Bothrops atrox snake venom myonecrosis |
description |
A myotoxin from Bothrops atrox snake venom was purified by cationic exchange on CM-Sephadex C-50 with 0,05M ammonium acetate pH 7. The myotoxin is a basic protein and by gel filtration and PAGE-SDS was demonstrated that protein has a molecular weight of 27 kDa and two polipeptides chain of 14 kDa each one. The inoculation of myotoxin in gastrocnemius muscle of white mice produce liberation of creatin kinase as well as myonecrosis. The myotoxin has phospholipasic, anticoagulant and edematic activity, but not hemolytic activity. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-07-15 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/2436 10.15381/rpb.v11i1.2436 |
url |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/2436 |
identifier_str_mv |
10.15381/rpb.v11i1.2436 |
dc.language.none.fl_str_mv |
spa |
language |
spa |
dc.relation.none.fl_str_mv |
https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/2436/2134 |
dc.rights.none.fl_str_mv |
Derechos de autor 2004 Sergio Huatuco, Enrique Escobar, Armando Yarlequé https://creativecommons.org/licenses/by-nc-sa/4.0 info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Derechos de autor 2004 Sergio Huatuco, Enrique Escobar, Armando Yarlequé https://creativecommons.org/licenses/by-nc-sa/4.0 |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas |
publisher.none.fl_str_mv |
Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas |
dc.source.none.fl_str_mv |
Revista Peruana de Biología; Vol. 11 Núm. 1 (2004); 79-86 Revista Peruana de Biología; Vol. 11 No. 1 (2004); 79-86 1727-9933 1561-0837 reponame:Revistas - Universidad Nacional Mayor de San Marcos instname:Universidad Nacional Mayor de San Marcos instacron:UNMSM |
instname_str |
Universidad Nacional Mayor de San Marcos |
instacron_str |
UNMSM |
institution |
UNMSM |
reponame_str |
Revistas - Universidad Nacional Mayor de San Marcos |
collection |
Revistas - Universidad Nacional Mayor de San Marcos |
repository.name.fl_str_mv |
|
repository.mail.fl_str_mv |
|
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1795238309135384576 |
score |
13.7211075 |
Nota importante:
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).
La información contenida en este registro es de entera responsabilidad de la institución que gestiona el repositorio institucional donde esta contenido este documento o set de datos. El CONCYTEC no se hace responsable por los contenidos (publicaciones y/o datos) accesibles a través del Repositorio Nacional Digital de Ciencia, Tecnología e Innovación de Acceso Abierto (ALICIA).