Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | |
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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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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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 |
repository.mail.fl_str_mv |
|
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1799136308492238848 |