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| Registros recuperados : 140 | |
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Registro Completo
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Biblioteca(s): |
Epagri-Sede. |
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Data corrente: |
20/04/2011 |
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Data da última atualização: |
20/04/2011 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
-- - -- |
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Autoria: |
SCHVEITZER, B.; FELIPPE, A. C.; B, A. D.; MINATTI, E.; ZANETTE, D.; LOPES, A. |
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Afiliação: |
Epagri |
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Título: |
Sodium dodecyl sulfate promoting a cooperative association process of sodium cholate with bovine serum albumin. |
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Ano de publicação: |
2006 |
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Fonte/Imprenta: |
Journal of Colloid and Interface Science Print, EUA, v. 298, n. , p. 457-466, 2006. |
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Idioma: |
Inglês |
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Notas: |
ISSN, 00219797 |
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Conteúdo: |
Sodium cholate (NaC) was used as a representative bile salt in the process of cooperative binding to bovine serum albumin (BSA) in a mixture with sodium dodecyl sulfate (SDS). The experiments were performed in 0.02 M Tris¨CHCl buffer solution (pH 7.50), in the presence of 0.1% BSA and at 25 ¡ãC. The aim of this study is to provide information on the performance of the BSA in the promotion of cooperative binding of sodium cholate promoted by the presence of SDS. The method used to monitor the binding was based on the analysis of the effect of SDS and NaC concentrations and their mixtures upon the fluorescence intensity of the BSA tryptophan residues. Plots of the fluorescence emission bands in terms of the A0/A ratio vs surfactant concentrations, where A0 and A represent the areas of emission bands in the presence and absence of the surfactants, respectively, were drawn in order to investigate the surfactant interaction with the protein. An alternative methodology, the specific conductivity vs surfactant concentration plots, was used, which involves mixtures of SDS and NaC to investigate the association processes, through the determination of the critical aggregation concentration (cac, when in the presence of protein) and the critical micellar concentration (cmc). The results led to a general conclusion that as the mixed micellar aggregates become richer in the bile salt monomer, the tendency to lose the reactivity with the protein increases. According to our results, a clear evidence of the predomination of BSA¨CSDS¨CNaC complexes is found only for the SDS molar fraction above ¡Ö0.6, and below this fraction a tendency toward free mixed micelles starts to predominate. MenosSodium cholate (NaC) was used as a representative bile salt in the process of cooperative binding to bovine serum albumin (BSA) in a mixture with sodium dodecyl sulfate (SDS). The experiments were performed in 0.02 M Tris¨CHCl buffer solution (pH 7.50), in the presence of 0.1% BSA and at 25 ¡ãC. The aim of this study is to provide information on the performance of the BSA in the promotion of cooperative binding of sodium cholate promoted by the presence of SDS. The method used to monitor the binding was based on the analysis of the effect of SDS and NaC concentrations and their mixtures upon the fluorescence intensity of the BSA tryptophan residues. Plots of the fluorescence emission bands in terms of the A0/A ratio vs surfactant concentrations, where A0 and A represent the areas of emission bands in the presence and absence of the surfactants, respectively, were drawn in order to investigate the surfactant interaction with the protein. An alternative methodology, the specific conductivity vs surfactant concentration plots, was used, which involves mixtures of SDS and NaC to investigate the association processes, through the determination of the critical aggregation concentration (cac, when in the presence of protein) and the critical micellar concentration (cmc). The results led to a general conclusion that as the mixed micellar aggregates become richer in the bile salt monomer, the tendency to lose the reactivity with the protein increases. According to our results, a clea... Mostrar Tudo |
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Palavras-Chave: |
Bovine serum albumin BSA Sodium cholate Proteinsurfactant interaction Anionic surfactant mixtures Fluorescence quenchin. |
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Categoria do assunto: |
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Marc: |
LEADER 02281naa a2200145 a 4500
001 1075883
005 2011-04-20
008 2006 bl uuuu u00u1 u #d
100 1 $aEpagri
245 $aSodium dodecyl sulfate promoting a cooperative association process of sodium cholate with bovine serum albumin.
260 $c2006
500 $aISSN, 00219797
520 $aSodium cholate (NaC) was used as a representative bile salt in the process of cooperative binding to bovine serum albumin (BSA) in a mixture with sodium dodecyl sulfate (SDS). The experiments were performed in 0.02 M Tris¨CHCl buffer solution (pH 7.50), in the presence of 0.1% BSA and at 25 ¡ãC. The aim of this study is to provide information on the performance of the BSA in the promotion of cooperative binding of sodium cholate promoted by the presence of SDS. The method used to monitor the binding was based on the analysis of the effect of SDS and NaC concentrations and their mixtures upon the fluorescence intensity of the BSA tryptophan residues. Plots of the fluorescence emission bands in terms of the A0/A ratio vs surfactant concentrations, where A0 and A represent the areas of emission bands in the presence and absence of the surfactants, respectively, were drawn in order to investigate the surfactant interaction with the protein. An alternative methodology, the specific conductivity vs surfactant concentration plots, was used, which involves mixtures of SDS and NaC to investigate the association processes, through the determination of the critical aggregation concentration (cac, when in the presence of protein) and the critical micellar concentration (cmc). The results led to a general conclusion that as the mixed micellar aggregates become richer in the bile salt monomer, the tendency to lose the reactivity with the protein increases. According to our results, a clear evidence of the predomination of BSA¨CSDS¨CNaC complexes is found only for the SDS molar fraction above ¡Ö0.6, and below this fraction a tendency toward free mixed micelles starts to predominate.
653 $aBovine serum albumin BSA Sodium cholate Proteinsurfactant interaction Anionic surfactant mixtures Fluorescence quenchin
773 $tJournal of Colloid and Interface Science Print, EUA$gv. 298, n. , p. 457-466, 2006.
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Epagri-Sede (Epagri-Sede) |
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