Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review

Detalhes bibliográficos
Autor(a) principal: Baracat-Pereira, Maria Cristina
Data de Publicação: 2011
Outros Autores: Barbosa, Meire de Oliveira, Magalhães Júnior, Marcos Jorge, Carrijo, Lanna Clicia, Games, Patrícia Dias, Almeida, Hebréia Oliveira, Sena Netto, José Fabiano, Pereira, Matheus Rodrigues, Barros, Everaldo Gonçalves de
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: http://dx.doi.org/10.1590/S1415-47572012000200009
http://www.locus.ufv.br/handle/123456789/12551
Resumo: The enrichment and isolation of proteins are considered limiting steps in proteomic studies. Identification of proteins whose expression is transient, those that are of low-abundance, and of natural peptides not described in databases, is still a great challenge. Plant extracts are in general complex, and contaminants interfere with the identification of proteins involved in important physiological processes, such as plant defense against pathogens. This review discusses the challenges and strategies of separomics applied to the identification of low-abundance proteins and peptides in plants, especially in plants challenged by pathogens. Separomics is described as a group of methodological strategies for the separation of protein molecules for proteomics. Several tools have been used to remove highly abundant proteins from samples and also non-protein contaminants. The use of chromatographic techniques, the partition of the proteome into subproteomes, and an effort to isolate proteins in their native form have allowed the isolation and identification of rare proteins involved in different processes.
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spelling Baracat-Pereira, Maria CristinaBarbosa, Meire de OliveiraMagalhães Júnior, Marcos JorgeCarrijo, Lanna CliciaGames, Patrícia DiasAlmeida, Hebréia OliveiraSena Netto, José FabianoPereira, Matheus RodriguesBarros, Everaldo Gonçalves de2017-10-30T17:23:08Z2017-10-30T17:23:08Z2011-01-241415-4757http://dx.doi.org/10.1590/S1415-47572012000200009http://www.locus.ufv.br/handle/123456789/12551The enrichment and isolation of proteins are considered limiting steps in proteomic studies. Identification of proteins whose expression is transient, those that are of low-abundance, and of natural peptides not described in databases, is still a great challenge. Plant extracts are in general complex, and contaminants interfere with the identification of proteins involved in important physiological processes, such as plant defense against pathogens. This review discusses the challenges and strategies of separomics applied to the identification of low-abundance proteins and peptides in plants, especially in plants challenged by pathogens. Separomics is described as a group of methodological strategies for the separation of protein molecules for proteomics. Several tools have been used to remove highly abundant proteins from samples and also non-protein contaminants. The use of chromatographic techniques, the partition of the proteome into subproteomes, and an effort to isolate proteins in their native form have allowed the isolation and identification of rare proteins involved in different processes.engGenetics and Molecular Biologyvol. 35, n. 1, supl. 1, p. 283-291, 2012Sample preparationComplex protein extractSubproteomesLow-abundance proteinsCell wall proteinsSeparomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a reviewinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALv35n1s1a09.pdfv35n1s1a09.pdftexto completoapplication/pdf623721https://locus.ufv.br//bitstream/123456789/12551/1/v35n1s1a09.pdfa21cf32f7fedff21a80e6a4f68eed5eaMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/12551/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILv35n1s1a09.pdf.jpgv35n1s1a09.pdf.jpgIM Thumbnailimage/jpeg5115https://locus.ufv.br//bitstream/123456789/12551/3/v35n1s1a09.pdf.jpge2635e98f48433147d03c4d458e267f9MD53123456789/125512017-10-30 22:01:01.633oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452017-10-31T01:01:01LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
title Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
spellingShingle Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
Baracat-Pereira, Maria Cristina
Sample preparation
Complex protein extract
Subproteomes
Low-abundance proteins
Cell wall proteins
title_short Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
title_full Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
title_fullStr Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
title_full_unstemmed Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
title_sort Separomics applied to the proteomics and peptidomics of low-abundance proteins: choice of methods and challenges - a review
author Baracat-Pereira, Maria Cristina
author_facet Baracat-Pereira, Maria Cristina
Barbosa, Meire de Oliveira
Magalhães Júnior, Marcos Jorge
Carrijo, Lanna Clicia
Games, Patrícia Dias
Almeida, Hebréia Oliveira
Sena Netto, José Fabiano
Pereira, Matheus Rodrigues
Barros, Everaldo Gonçalves de
author_role author
author2 Barbosa, Meire de Oliveira
Magalhães Júnior, Marcos Jorge
Carrijo, Lanna Clicia
Games, Patrícia Dias
Almeida, Hebréia Oliveira
Sena Netto, José Fabiano
Pereira, Matheus Rodrigues
Barros, Everaldo Gonçalves de
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Baracat-Pereira, Maria Cristina
Barbosa, Meire de Oliveira
Magalhães Júnior, Marcos Jorge
Carrijo, Lanna Clicia
Games, Patrícia Dias
Almeida, Hebréia Oliveira
Sena Netto, José Fabiano
Pereira, Matheus Rodrigues
Barros, Everaldo Gonçalves de
dc.subject.pt-BR.fl_str_mv Sample preparation
Complex protein extract
Subproteomes
Low-abundance proteins
Cell wall proteins
topic Sample preparation
Complex protein extract
Subproteomes
Low-abundance proteins
Cell wall proteins
description The enrichment and isolation of proteins are considered limiting steps in proteomic studies. Identification of proteins whose expression is transient, those that are of low-abundance, and of natural peptides not described in databases, is still a great challenge. Plant extracts are in general complex, and contaminants interfere with the identification of proteins involved in important physiological processes, such as plant defense against pathogens. This review discusses the challenges and strategies of separomics applied to the identification of low-abundance proteins and peptides in plants, especially in plants challenged by pathogens. Separomics is described as a group of methodological strategies for the separation of protein molecules for proteomics. Several tools have been used to remove highly abundant proteins from samples and also non-protein contaminants. The use of chromatographic techniques, the partition of the proteome into subproteomes, and an effort to isolate proteins in their native form have allowed the isolation and identification of rare proteins involved in different processes.
publishDate 2011
dc.date.issued.fl_str_mv 2011-01-24
dc.date.accessioned.fl_str_mv 2017-10-30T17:23:08Z
dc.date.available.fl_str_mv 2017-10-30T17:23:08Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1590/S1415-47572012000200009
http://www.locus.ufv.br/handle/123456789/12551
dc.identifier.issn.none.fl_str_mv 1415-4757
identifier_str_mv 1415-4757
url http://dx.doi.org/10.1590/S1415-47572012000200009
http://www.locus.ufv.br/handle/123456789/12551
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv vol. 35, n. 1, supl. 1, p. 283-291, 2012
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dc.publisher.none.fl_str_mv Genetics and Molecular Biology
publisher.none.fl_str_mv Genetics and Molecular Biology
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