Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom
- Autores
- Maruñak, Silvana Licia; Leiva, Laura Cristina Ana; García Denegri, María Emilia; Teibler, Gladys Pamela; Acosta, Ofelia Cristina
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Maruñak, Silvana Licia. Universidad Nacional del Nordeste. Facultad de Ciencias. Veterinarias; Argentina.
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina.
Fil: García Denegri, María Emilia. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina.
Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina.
Fil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina.
A phospholipase A2 has been isolated from Bothrops jararacussu venom from snakes that inhabit the northeast region of Argentina. The present study describes in vivo and in vitro biological activities of phospholipase A2 from B. jararacussu as well as isolation details of its. Venom was obtained by milking of adult snakes which were housing in wood reptile cages of varying dimensions in heated (20–30oC) rooms. Snakes received a weekly diet of mice and water was available ad libitum for drinking and soaking. The enzyme was purified by gel filtration on a Sephadex G-75 column followed by ion exchange chromatography on a SP-Sephadex C25 column. The major peak belonging to proteins was retained in the cation exchanger and then eluted using a concentration gradient of KCl that exhibited phospholipase activity. This basic PLA2 consists of a single polypeptide chain with a molecular mass of 15.6 kDa. It had a high indirect hemolytic activity and produced a significant paw edema reaction in mice. The enzyme showed a low lethality (LD50 148.6 μg) when was administered i.p. but exhibited elevated myotoxic effects in vivo by increasing plasma CK activity of injected mice, corroborated results by the histological observations of samples of gastrocnemius muscle. Myonecrosis is the result of intense destruction of muscular fibers that involves local infiltration of inflammatory cells and leads to the highest peak of CK level just after 1 hour mice injection. Moreover, the isolated enzyme showed anticoagulant activity, evaluated on sheep platelet-poor plasma which recalcification time was prolonged after incubation with the isolated phospholipase A2 . These findings showed that this phospholipase, isolated by only two simple chromatographic steps, possesses high edematogenic and myotoxic activities. However, despite the low lethal activity, this enzyme would contribute markedly to the pathophysiology of the bothropic envenomation. - Fuente
- Biocell, 2007, vol. 31, no. 3, p. 355-364.
- Materia
-
Snake venom
Bothrops jararacussu
Phospholipase A2
Isolation - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Universidad Nacional del Nordeste
- OAI Identificador
- oai:repositorio.unne.edu.ar:123456789/48609
Ver los metadatos del registro completo
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Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venomMaruñak, Silvana LiciaLeiva, Laura Cristina AnaGarcía Denegri, María EmiliaTeibler, Gladys PamelaAcosta, Ofelia CristinaSnake venomBothrops jararacussuPhospholipase A2IsolationFil: Maruñak, Silvana Licia. Universidad Nacional del Nordeste. Facultad de Ciencias. Veterinarias; Argentina.Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina.Fil: García Denegri, María Emilia. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina.Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina.Fil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina.A phospholipase A2 has been isolated from Bothrops jararacussu venom from snakes that inhabit the northeast region of Argentina. The present study describes in vivo and in vitro biological activities of phospholipase A2 from B. jararacussu as well as isolation details of its. Venom was obtained by milking of adult snakes which were housing in wood reptile cages of varying dimensions in heated (20–30oC) rooms. Snakes received a weekly diet of mice and water was available ad libitum for drinking and soaking. The enzyme was purified by gel filtration on a Sephadex G-75 column followed by ion exchange chromatography on a SP-Sephadex C25 column. The major peak belonging to proteins was retained in the cation exchanger and then eluted using a concentration gradient of KCl that exhibited phospholipase activity. This basic PLA2 consists of a single polypeptide chain with a molecular mass of 15.6 kDa. It had a high indirect hemolytic activity and produced a significant paw edema reaction in mice. The enzyme showed a low lethality (LD50 148.6 μg) when was administered i.p. but exhibited elevated myotoxic effects in vivo by increasing plasma CK activity of injected mice, corroborated results by the histological observations of samples of gastrocnemius muscle. Myonecrosis is the result of intense destruction of muscular fibers that involves local infiltration of inflammatory cells and leads to the highest peak of CK level just after 1 hour mice injection. Moreover, the isolated enzyme showed anticoagulant activity, evaluated on sheep platelet-poor plasma which recalcification time was prolonged after incubation with the isolated phospholipase A2 . These findings showed that this phospholipase, isolated by only two simple chromatographic steps, possesses high edematogenic and myotoxic activities. However, despite the low lethal activity, this enzyme would contribute markedly to the pathophysiology of the bothropic envenomation.Sociedad Latinoamericana de Microscopia Electrónica2007-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfMaruñak, Silvana Licia, et al., 2007. Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom. Biocell. Mendoza: Sociedad Latinoamericana de Microscopia Electrónica, vol. 31, no. 3, p. 355-364. e-ISSN 1667-5746.0327-9545http://repositorio.unne.edu.ar/handle/123456789/48609Biocell, 2007, vol. 31, no. 3, p. 355-364.reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)instname:Universidad Nacional del Nordesteenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/2.5/ar/Atribución-NoComercial-SinDerivadas 2.5 Argentina2025-09-04T11:14:08Zoai:repositorio.unne.edu.ar:123456789/48609instacron:UNNEInstitucionalhttp://repositorio.unne.edu.ar/Universidad públicaNo correspondehttp://repositorio.unne.edu.ar/oaiososa@bib.unne.edu.ar;sergio.alegria@unne.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:48712025-09-04 11:14:08.828Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordestefalse |
dc.title.none.fl_str_mv |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
title |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
spellingShingle |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom Maruñak, Silvana Licia Snake venom Bothrops jararacussu Phospholipase A2 Isolation |
title_short |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
title_full |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
title_fullStr |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
title_full_unstemmed |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
title_sort |
Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom |
dc.creator.none.fl_str_mv |
Maruñak, Silvana Licia Leiva, Laura Cristina Ana García Denegri, María Emilia Teibler, Gladys Pamela Acosta, Ofelia Cristina |
author |
Maruñak, Silvana Licia |
author_facet |
Maruñak, Silvana Licia Leiva, Laura Cristina Ana García Denegri, María Emilia Teibler, Gladys Pamela Acosta, Ofelia Cristina |
author_role |
author |
author2 |
Leiva, Laura Cristina Ana García Denegri, María Emilia Teibler, Gladys Pamela Acosta, Ofelia Cristina |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Snake venom Bothrops jararacussu Phospholipase A2 Isolation |
topic |
Snake venom Bothrops jararacussu Phospholipase A2 Isolation |
dc.description.none.fl_txt_mv |
Fil: Maruñak, Silvana Licia. Universidad Nacional del Nordeste. Facultad de Ciencias. Veterinarias; Argentina. Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina. Fil: García Denegri, María Emilia. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura; Argentina. Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina. Fil: Acosta, Ofelia Cristina. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina. A phospholipase A2 has been isolated from Bothrops jararacussu venom from snakes that inhabit the northeast region of Argentina. The present study describes in vivo and in vitro biological activities of phospholipase A2 from B. jararacussu as well as isolation details of its. Venom was obtained by milking of adult snakes which were housing in wood reptile cages of varying dimensions in heated (20–30oC) rooms. Snakes received a weekly diet of mice and water was available ad libitum for drinking and soaking. The enzyme was purified by gel filtration on a Sephadex G-75 column followed by ion exchange chromatography on a SP-Sephadex C25 column. The major peak belonging to proteins was retained in the cation exchanger and then eluted using a concentration gradient of KCl that exhibited phospholipase activity. This basic PLA2 consists of a single polypeptide chain with a molecular mass of 15.6 kDa. It had a high indirect hemolytic activity and produced a significant paw edema reaction in mice. The enzyme showed a low lethality (LD50 148.6 μg) when was administered i.p. but exhibited elevated myotoxic effects in vivo by increasing plasma CK activity of injected mice, corroborated results by the histological observations of samples of gastrocnemius muscle. Myonecrosis is the result of intense destruction of muscular fibers that involves local infiltration of inflammatory cells and leads to the highest peak of CK level just after 1 hour mice injection. Moreover, the isolated enzyme showed anticoagulant activity, evaluated on sheep platelet-poor plasma which recalcification time was prolonged after incubation with the isolated phospholipase A2 . These findings showed that this phospholipase, isolated by only two simple chromatographic steps, possesses high edematogenic and myotoxic activities. However, despite the low lethal activity, this enzyme would contribute markedly to the pathophysiology of the bothropic envenomation. |
description |
Fil: Maruñak, Silvana Licia. Universidad Nacional del Nordeste. Facultad de Ciencias. Veterinarias; Argentina. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
Maruñak, Silvana Licia, et al., 2007. Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom. Biocell. Mendoza: Sociedad Latinoamericana de Microscopia Electrónica, vol. 31, no. 3, p. 355-364. e-ISSN 1667-5746. 0327-9545 http://repositorio.unne.edu.ar/handle/123456789/48609 |
identifier_str_mv |
Maruñak, Silvana Licia, et al., 2007. Isolation and biological characterization of a basic phospholipase A2 from bothrops jararacussu snake venom. Biocell. Mendoza: Sociedad Latinoamericana de Microscopia Electrónica, vol. 31, no. 3, p. 355-364. e-ISSN 1667-5746. 0327-9545 |
url |
http://repositorio.unne.edu.ar/handle/123456789/48609 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Atribución-NoComercial-SinDerivadas 2.5 Argentina |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Atribución-NoComercial-SinDerivadas 2.5 Argentina |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Sociedad Latinoamericana de Microscopia Electrónica |
publisher.none.fl_str_mv |
Sociedad Latinoamericana de Microscopia Electrónica |
dc.source.none.fl_str_mv |
Biocell, 2007, vol. 31, no. 3, p. 355-364. reponame:Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) instname:Universidad Nacional del Nordeste |
reponame_str |
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) |
collection |
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) |
instname_str |
Universidad Nacional del Nordeste |
repository.name.fl_str_mv |
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) - Universidad Nacional del Nordeste |
repository.mail.fl_str_mv |
ososa@bib.unne.edu.ar;sergio.alegria@unne.edu.ar |
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1842344214220767232 |
score |
12.623145 |