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

Detalhes bibliográficos
Autor(a) principal: Gómez,GN
Data de Publicação: 2012
Outros Autores: Nerli,BB, Acosta,OC, Picó,GA, Leiva,LCA
Tipo de documento: Artigo
Idioma: eng
Título da fonte: The Journal of venomous animals and toxins including tropical diseases (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008
Resumo: 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.
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spelling An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systemspartitionsnake toxinsisolationphospholipase A2proteasesSnake 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.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2012-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008Journal of Venomous Animals and Toxins including Tropical Diseases v.18 n.3 2012reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/S1678-91992012000300008info:eu-repo/semantics/openAccessGómez,GNNerli,BBAcosta,OCPicó,GALeiva,LCAeng2012-09-14T00:00:00Zoai:scielo:S1678-91992012000300008Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2012-09-14T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
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
Gómez,GN
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
author Gómez,GN
author_facet Gómez,GN
Nerli,BB
Acosta,OC
Picó,GA
Leiva,LCA
author_role author
author2 Nerli,BB
Acosta,OC
Picó,GA
Leiva,LCA
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Gómez,GN
Nerli,BB
Acosta,OC
Picó,GA
Leiva,LCA
dc.subject.por.fl_str_mv partition
snake toxins
isolation
phospholipase A2
proteases
topic partition
snake toxins
isolation
phospholipase A2
proteases
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 2012-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1678-91992012000300008
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
dc.source.none.fl_str_mv Journal of Venomous Animals and Toxins including Tropical Diseases v.18 n.3 2012
reponame:The Journal of venomous animals and toxins including tropical diseases (Online)
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str The Journal of venomous animals and toxins including tropical diseases (Online)
collection The Journal of venomous animals and toxins including tropical diseases (Online)
repository.name.fl_str_mv The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv ||editorial@jvat.org.br
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