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
Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
Institución
Universidad Nacional del Nordeste
OAI Identificador
oai:repositorio.unne.edu.ar:123456789/48609

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network_acronym_str RIUNNE
repository_id_str 4871
network_name_str Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
spelling 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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