Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system
Autor(a) principal: | |
---|---|
Data de Publicação: | 2008 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.6/12313 |
Resumo: | A panel of four hydrophobic adsorbents (butyl-, octyl-, phenyl- and epoxy-Sepharose) was used to examine the selectivity and fractionation of several proteose peptone 3 (PP3) forms from a freeze-dried extract of whey bovine milk. In particular, the effects of altering the ligand type and salt were investigated. The chromatographic studies suggest that PP3 strongly interacts among the three commercial hydrophobic resins leading to a drop off in selectivity, while a complete binding was achieved at low salt concentrations (below 0.5 M) and total elution only with phosphate buffer and/or water stepwise conditions. Only in epoxy–Sepharose was an appreciably selectivity of the several fractions of PP3 present in the initial feedstock attained. Despite the high salt concentration for a complete binding of PP3 (above 1.5 M ammonium sulfate) onto this support, the dual salt system (ammonium sulfate 1 M and sodium citrate 0.8 M) led to a high separation degree of high and low molecular weight forms of PP3. |
id |
RCAP_20030d5c1d9dc811af53dce5b803609b |
---|---|
oai_identifier_str |
oai:ubibliorum.ubi.pt:10400.6/12313 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt systemProteose peptone 3Hydrophobic adsorbentsDual salt systemA panel of four hydrophobic adsorbents (butyl-, octyl-, phenyl- and epoxy-Sepharose) was used to examine the selectivity and fractionation of several proteose peptone 3 (PP3) forms from a freeze-dried extract of whey bovine milk. In particular, the effects of altering the ligand type and salt were investigated. The chromatographic studies suggest that PP3 strongly interacts among the three commercial hydrophobic resins leading to a drop off in selectivity, while a complete binding was achieved at low salt concentrations (below 0.5 M) and total elution only with phosphate buffer and/or water stepwise conditions. Only in epoxy–Sepharose was an appreciably selectivity of the several fractions of PP3 present in the initial feedstock attained. Despite the high salt concentration for a complete binding of PP3 (above 1.5 M ammonium sulfate) onto this support, the dual salt system (ammonium sulfate 1 M and sodium citrate 0.8 M) led to a high separation degree of high and low molecular weight forms of PP3.John Wiley & Sons, LtduBibliorumSousa, Ângela Maria Almeida dePassarinha, Luís António PaulinoRodrigues, L.R.Teixeira, JoséMendonça, AntónioQueiroz, João2022-08-24T10:20:24Z2008-01-182008-01-18T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.6/12313engSousa, A., Passarinha, L. A., Rodrigues, L. R., Teixeira, J. A., Mendonça, A., & Queiroz, J. A. (2008). Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system. Biomedical Chromatography, 22(5), 447-449. doi:10.1002/bmc.96110.1002/bmc.961metadata only accessinfo: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:RCAAP2024-03-06T02:30:35Zoai:ubibliorum.ubi.pt:10400.6/12313Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:51:57.060866Repositório 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 |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
title |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
spellingShingle |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system Sousa, Ângela Maria Almeida de Proteose peptone 3 Hydrophobic adsorbents Dual salt system |
title_short |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
title_full |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
title_fullStr |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
title_full_unstemmed |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
title_sort |
Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system |
author |
Sousa, Ângela Maria Almeida de |
author_facet |
Sousa, Ângela Maria Almeida de Passarinha, Luís António Paulino Rodrigues, L.R. Teixeira, José Mendonça, António Queiroz, João |
author_role |
author |
author2 |
Passarinha, Luís António Paulino Rodrigues, L.R. Teixeira, José Mendonça, António Queiroz, João |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
uBibliorum |
dc.contributor.author.fl_str_mv |
Sousa, Ângela Maria Almeida de Passarinha, Luís António Paulino Rodrigues, L.R. Teixeira, José Mendonça, António Queiroz, João |
dc.subject.por.fl_str_mv |
Proteose peptone 3 Hydrophobic adsorbents Dual salt system |
topic |
Proteose peptone 3 Hydrophobic adsorbents Dual salt system |
description |
A panel of four hydrophobic adsorbents (butyl-, octyl-, phenyl- and epoxy-Sepharose) was used to examine the selectivity and fractionation of several proteose peptone 3 (PP3) forms from a freeze-dried extract of whey bovine milk. In particular, the effects of altering the ligand type and salt were investigated. The chromatographic studies suggest that PP3 strongly interacts among the three commercial hydrophobic resins leading to a drop off in selectivity, while a complete binding was achieved at low salt concentrations (below 0.5 M) and total elution only with phosphate buffer and/or water stepwise conditions. Only in epoxy–Sepharose was an appreciably selectivity of the several fractions of PP3 present in the initial feedstock attained. Despite the high salt concentration for a complete binding of PP3 (above 1.5 M ammonium sulfate) onto this support, the dual salt system (ammonium sulfate 1 M and sodium citrate 0.8 M) led to a high separation degree of high and low molecular weight forms of PP3. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-01-18 2008-01-18T00:00:00Z 2022-08-24T10:20:24Z |
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 |
http://hdl.handle.net/10400.6/12313 |
url |
http://hdl.handle.net/10400.6/12313 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Sousa, A., Passarinha, L. A., Rodrigues, L. R., Teixeira, J. A., Mendonça, A., & Queiroz, J. A. (2008). Separation of different forms of proteose peptone 3 by hydrophobic interaction chromatography with a dual salt system. Biomedical Chromatography, 22(5), 447-449. doi:10.1002/bmc.961 10.1002/bmc.961 |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
metadata only access |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
John Wiley & Sons, Ltd |
publisher.none.fl_str_mv |
John Wiley & Sons, Ltd |
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 |
|
_version_ |
1799136408051384320 |