An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

Autores
Gomez, Gabriela Noemi; Nerli, Bibiana Beatriz; Acosta, Ofelia Cristina; Picó, Guillermo Alfredo; Leiva, Laura Cristina Ana
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.
Fil: Gomez, Gabriela Noemi. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Acosta, Ofelia Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional del Nordeste; Argentina
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Materia
PARTITION
SNAKE TOXINS
ISOLATION
PHOSPHOLIPASE A2
PROTEASES
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/196922
Acceder
id CONICETDig_28e5f70f5e027d8a1f3dd968407140b8
oai_identifier_str oai:ri.conicet.gov.ar:11336/196922
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systemsGomez, Gabriela NoemiNerli, Bibiana BeatrizAcosta, Ofelia CristinaPicó, Guillermo AlfredoLeiva, Laura Cristina AnaPARTITIONSNAKE TOXINSISOLATIONPHOSPHOLIPASE A2PROTEASEShttps://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.Fil: Gomez, Gabriela Noemi. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; ArgentinaFil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Acosta, Ofelia Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional del Nordeste; ArgentinaFil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; ArgentinaCevap-unesp2012-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/196922Gomez, Gabriela Noemi; Nerli, Bibiana Beatriz; Acosta, Ofelia Cristina; Picó, Guillermo Alfredo; Leiva, Laura Cristina Ana; An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems; Cevap-unesp; Journal Of Venomous Animals And Toxins Including Tropical Diseases; 18; 3; 8-2012; 306-3161678-9199CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.scielo.br/scielo.php?pid=S1678-91992012000300008&script=sci_arttextinfo:eu-repo/semantics/altIdentifier/doi/10.1590/S1678-91992012000300008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:05:21Zoai:ri.conicet.gov.ar:11336/196922instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:05:21.798CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
title An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
spellingShingle An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
Gomez, Gabriela Noemi
PARTITION
SNAKE TOXINS
ISOLATION
PHOSPHOLIPASE A2
PROTEASES
title_short An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
title_full An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
title_fullStr An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
title_full_unstemmed An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
title_sort An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems
dc.creator.none.fl_str_mv Gomez, Gabriela Noemi
Nerli, Bibiana Beatriz
Acosta, Ofelia Cristina
Picó, Guillermo Alfredo
Leiva, Laura Cristina Ana
author Gomez, Gabriela Noemi
author_facet Gomez, Gabriela Noemi
Nerli, Bibiana Beatriz
Acosta, Ofelia Cristina
Picó, Guillermo Alfredo
Leiva, Laura Cristina Ana
author_role author
author2 Nerli, Bibiana Beatriz
Acosta, Ofelia Cristina
Picó, Guillermo Alfredo
Leiva, Laura Cristina Ana
author2_role author
author
author
author
dc.subject.none.fl_str_mv PARTITION
SNAKE TOXINS
ISOLATION
PHOSPHOLIPASE A2
PROTEASES
topic PARTITION
SNAKE TOXINS
ISOLATION
PHOSPHOLIPASE A2
PROTEASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.7
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.
Fil: Gomez, Gabriela Noemi. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Acosta, Ofelia Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional del Nordeste; Argentina
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
description Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the homogeneity of the isolated proteins.
publishDate 2012
dc.date.none.fl_str_mv 2012-08
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 http://hdl.handle.net/11336/196922
Gomez, Gabriela Noemi; Nerli, Bibiana Beatriz; Acosta, Ofelia Cristina; Picó, Guillermo Alfredo; Leiva, Laura Cristina Ana; An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems; Cevap-unesp; Journal Of Venomous Animals And Toxins Including Tropical Diseases; 18; 3; 8-2012; 306-316
1678-9199
CONICET Digital
CONICET
url http://hdl.handle.net/11336/196922
identifier_str_mv Gomez, Gabriela Noemi; Nerli, Bibiana Beatriz; Acosta, Ofelia Cristina; Picó, Guillermo Alfredo; Leiva, Laura Cristina Ana; An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems; Cevap-unesp; Journal Of Venomous Animals And Toxins Including Tropical Diseases; 18; 3; 8-2012; 306-316
1678-9199
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.scielo.br/scielo.php?pid=S1678-91992012000300008&script=sci_arttext
info:eu-repo/semantics/altIdentifier/doi/10.1590/S1678-91992012000300008
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cevap-unesp
publisher.none.fl_str_mv Cevap-unesp
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842980194842836992
score 12.993085

Publicaciones similares