Fractionation of secalins and hordeins by preparative electrophoresis at acid pH

Autores
Rumbo, Martín; Margheritis, Analía; Chirdo, Fernando Gabriel; Giorgieri, Sergio Alejandro; Fossati, Carlos A.; Añón, María Cristina
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this report, the optimization of a preparative electrophoretic method to fractionate secalins and hordeins is described. Separation was performed in preparative 7% polyacrylamide gels of 4 cm length at pH 3.1. The separation performance was tested using analytical electrophoresis at pH 3.1 and capillary electrophoresis (CE). Fractions of B- and C-hordeins were isolated in a single run from barley ethanol extract. γ- and ω-secalin fractions were isolated from rye ethanol extract. Resolution of preparative separation was maintained at a protein load of up to 30 mg in each run. Each secalin and hordein fraction showed several components of close mobility when analyzed by CE. Fractions from the preparative separation were pooled in such a way that no components from one pool were present in the others. These pooled fractions could be used as starting material for single polypeptide purification. Preparative electrophoresis at low pH allowed a simple separation of γ- and ω-secalins and B- and C-hordeins from crude material under non-denaturing conditions.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Química
Secalin
Hordein
Preparative electrophoresis
Polyacrylamide gel electrophoresis at pH 3.1
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/143628
Acceder
id SEDICI_4e5856dd04474422fc1dbea4e22f9309
oai_identifier_str oai:sedici.unlp.edu.ar:10915/143628
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Fractionation of secalins and hordeins by preparative electrophoresis at acid pHRumbo, MartínMargheritis, AnalíaChirdo, Fernando GabrielGiorgieri, Sergio AlejandroFossati, Carlos A.Añón, María CristinaQuímicaSecalinHordeinPreparative electrophoresisPolyacrylamide gel electrophoresis at pH 3.1In this report, the optimization of a preparative electrophoretic method to fractionate secalins and hordeins is described. Separation was performed in preparative 7% polyacrylamide gels of 4 cm length at pH 3.1. The separation performance was tested using analytical electrophoresis at pH 3.1 and capillary electrophoresis (CE). Fractions of B- and C-hordeins were isolated in a single run from barley ethanol extract. γ- and ω-secalin fractions were isolated from rye ethanol extract. Resolution of preparative separation was maintained at a protein load of up to 30 mg in each run. Each secalin and hordein fraction showed several components of close mobility when analyzed by CE. Fractions from the preparative separation were pooled in such a way that no components from one pool were present in the others. These pooled fractions could be used as starting material for single polypeptide purification. Preparative electrophoresis at low pH allowed a simple separation of γ- and ω-secalins and B- and C-hordeins from crude material under non-denaturing conditions.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2002-01-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf198-201http://sedici.unlp.edu.ar/handle/10915/143628enginfo:eu-repo/semantics/altIdentifier/issn/1438-2377info:eu-repo/semantics/altIdentifier/issn/1438-2385info:eu-repo/semantics/altIdentifier/doi/10.1007/s00217-001-0441-6info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:13:10Zoai:sedici.unlp.edu.ar:10915/143628Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:13:11.231SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
title Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
spellingShingle Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
Rumbo, Martín
Química
Secalin
Hordein
Preparative electrophoresis
Polyacrylamide gel electrophoresis at pH 3.1
title_short Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
title_full Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
title_fullStr Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
title_full_unstemmed Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
title_sort Fractionation of secalins and hordeins by preparative electrophoresis at acid pH
dc.creator.none.fl_str_mv Rumbo, Martín
Margheritis, Analía
Chirdo, Fernando Gabriel
Giorgieri, Sergio Alejandro
Fossati, Carlos A.
Añón, María Cristina
author Rumbo, Martín
author_facet Rumbo, Martín
Margheritis, Analía
Chirdo, Fernando Gabriel
Giorgieri, Sergio Alejandro
Fossati, Carlos A.
Añón, María Cristina
author_role author
author2 Margheritis, Analía
Chirdo, Fernando Gabriel
Giorgieri, Sergio Alejandro
Fossati, Carlos A.
Añón, María Cristina
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Química
Secalin
Hordein
Preparative electrophoresis
Polyacrylamide gel electrophoresis at pH 3.1
topic Química
Secalin
Hordein
Preparative electrophoresis
Polyacrylamide gel electrophoresis at pH 3.1
dc.description.none.fl_txt_mv In this report, the optimization of a preparative electrophoretic method to fractionate secalins and hordeins is described. Separation was performed in preparative 7% polyacrylamide gels of 4 cm length at pH 3.1. The separation performance was tested using analytical electrophoresis at pH 3.1 and capillary electrophoresis (CE). Fractions of B- and C-hordeins were isolated in a single run from barley ethanol extract. γ- and ω-secalin fractions were isolated from rye ethanol extract. Resolution of preparative separation was maintained at a protein load of up to 30 mg in each run. Each secalin and hordein fraction showed several components of close mobility when analyzed by CE. Fractions from the preparative separation were pooled in such a way that no components from one pool were present in the others. These pooled fractions could be used as starting material for single polypeptide purification. Preparative electrophoresis at low pH allowed a simple separation of γ- and ω-secalins and B- and C-hordeins from crude material under non-denaturing conditions.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description In this report, the optimization of a preparative electrophoretic method to fractionate secalins and hordeins is described. Separation was performed in preparative 7% polyacrylamide gels of 4 cm length at pH 3.1. The separation performance was tested using analytical electrophoresis at pH 3.1 and capillary electrophoresis (CE). Fractions of B- and C-hordeins were isolated in a single run from barley ethanol extract. γ- and ω-secalin fractions were isolated from rye ethanol extract. Resolution of preparative separation was maintained at a protein load of up to 30 mg in each run. Each secalin and hordein fraction showed several components of close mobility when analyzed by CE. Fractions from the preparative separation were pooled in such a way that no components from one pool were present in the others. These pooled fractions could be used as starting material for single polypeptide purification. Preparative electrophoresis at low pH allowed a simple separation of γ- and ω-secalins and B- and C-hordeins from crude material under non-denaturing conditions.
publishDate 2002
dc.date.none.fl_str_mv 2002-01-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/143628
url http://sedici.unlp.edu.ar/handle/10915/143628
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1438-2377
info:eu-repo/semantics/altIdentifier/issn/1438-2385
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00217-001-0441-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
198-201
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 12.982451

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