Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing

Detalhes bibliográficos
Autor(a) principal: Ferreira, Renata A.
Data de Publicação: 2016
Outros Autores: Martins-Dias, Susete
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/20.500.12207/6045
Resumo: An alternative approach for plant complex protein extracts pre-purification by in-solution isoelectric focusing in non-denaturing conditions is presented. The separation of biologically active proteins, in narrow ranges of isoelectric point (pI) was obtained by a modified OFFGEL electrophoresis. Two different water-soluble protein extracts from Phragmites leaves were fractionated into 24 fractions within a 3-10 pI range at 10 °C in the absence of denaturing/reducing agents. One-dimensional electrophoretic analysis revealed different protein distribution patterns and the effective fractionation of both protein extracts. Peroxidase activity of each fraction confirmed that proteins remained active and pre-purification occurred. Biological triplicates assured the needed reproducibility.
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spelling Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusingIsoelectric focusingPlant extractsPlant leavesPlant proteinsPoaceaeAn alternative approach for plant complex protein extracts pre-purification by in-solution isoelectric focusing in non-denaturing conditions is presented. The separation of biologically active proteins, in narrow ranges of isoelectric point (pI) was obtained by a modified OFFGEL electrophoresis. Two different water-soluble protein extracts from Phragmites leaves were fractionated into 24 fractions within a 3-10 pI range at 10 °C in the absence of denaturing/reducing agents. One-dimensional electrophoretic analysis revealed different protein distribution patterns and the effective fractionation of both protein extracts. Peroxidase activity of each fraction confirmed that proteins remained active and pre-purification occurred. Biological triplicates assured the needed reproducibility.Elsevier2023-11-21T12:15:01Z2016-09-15T00:00:00Z2016-09-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.12207/6045eng0003-2697https://dx.doi.org/10.1016/j.ab.2016.07.004Ferreira, Renata A.Martins-Dias, Suseteinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-30T07:54:46Zoai:repositorio.ipbeja.pt:20.500.12207/6045Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:40:21.079595Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
title Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
spellingShingle Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
Ferreira, Renata A.
Isoelectric focusing
Plant extracts
Plant leaves
Plant proteins
Poaceae
title_short Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
title_full Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
title_fullStr Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
title_full_unstemmed Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
title_sort Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
author Ferreira, Renata A.
author_facet Ferreira, Renata A.
Martins-Dias, Susete
author_role author
author2 Martins-Dias, Susete
author2_role author
dc.contributor.author.fl_str_mv Ferreira, Renata A.
Martins-Dias, Susete
dc.subject.por.fl_str_mv Isoelectric focusing
Plant extracts
Plant leaves
Plant proteins
Poaceae
topic Isoelectric focusing
Plant extracts
Plant leaves
Plant proteins
Poaceae
description An alternative approach for plant complex protein extracts pre-purification by in-solution isoelectric focusing in non-denaturing conditions is presented. The separation of biologically active proteins, in narrow ranges of isoelectric point (pI) was obtained by a modified OFFGEL electrophoresis. Two different water-soluble protein extracts from Phragmites leaves were fractionated into 24 fractions within a 3-10 pI range at 10 °C in the absence of denaturing/reducing agents. One-dimensional electrophoretic analysis revealed different protein distribution patterns and the effective fractionation of both protein extracts. Peroxidase activity of each fraction confirmed that proteins remained active and pre-purification occurred. Biological triplicates assured the needed reproducibility.
publishDate 2016
dc.date.none.fl_str_mv 2016-09-15T00:00:00Z
2016-09-15
2023-11-21T12:15:01Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/20.500.12207/6045
url https://hdl.handle.net/20.500.12207/6045
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0003-2697
https://dx.doi.org/10.1016/j.ab.2016.07.004
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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