Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532009001000003 |
Resumo: | Thermodynamic studies of the effect of temperature (27-47 ºC) on the structure of bovine b-lactoglobulin-A (BLG-A) in the absence and presence of Cr(III) containing 50 mmol L-1 sodium chloride have been carried out using UV-Visible absorption spectroscopy, far and near circular dichroism (CD) and fluorescence spectroscopy. The far-UV CD studies do not show any significant change in the secondary structure of the protein at different temperatures in the absence and presence of Cr(III). On the contrary, the near-UV CD studies show change in the tertiary structure of the native BLG on increasing the temperature, indicating the exposure of Tyr residues. Fluorescence spectroscopic studies on the native BLG-A in the absence and presence of Cr(III) represent considerable change in the tertiary structure of the protein due to the increase in temperature. Due to protein stabilization in the presence of Cr(III) ions, the tertiary structure of BLG represents considerable alterations at 37 and 47 ο C that is in agreement with increasing of Tm values at these temperatures. |
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Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-Aβ-lactoglobulintemperatureCr(III) ionstertiary structureTm valueThermodynamic studies of the effect of temperature (27-47 ºC) on the structure of bovine b-lactoglobulin-A (BLG-A) in the absence and presence of Cr(III) containing 50 mmol L-1 sodium chloride have been carried out using UV-Visible absorption spectroscopy, far and near circular dichroism (CD) and fluorescence spectroscopy. The far-UV CD studies do not show any significant change in the secondary structure of the protein at different temperatures in the absence and presence of Cr(III). On the contrary, the near-UV CD studies show change in the tertiary structure of the native BLG on increasing the temperature, indicating the exposure of Tyr residues. Fluorescence spectroscopic studies on the native BLG-A in the absence and presence of Cr(III) represent considerable change in the tertiary structure of the protein due to the increase in temperature. Due to protein stabilization in the presence of Cr(III) ions, the tertiary structure of BLG represents considerable alterations at 37 and 47 ο C that is in agreement with increasing of Tm values at these temperatures.Sociedade Brasileira de Química2009-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532009001000003Journal of the Brazilian Chemical Society v.20 n.10 2009reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532009001000003info:eu-repo/semantics/openAccessDivsalar,AdelehSaboury,Ali AkbarAhmad,FaizanMoosavi-Movahedi,Ali Akbareng2011-10-14T00:00:00Zoai:scielo:S0103-50532009001000003Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2011-10-14T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
title |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
spellingShingle |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A Divsalar,Adeleh β-lactoglobulin temperature Cr(III) ions tertiary structure Tm value |
title_short |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
title_full |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
title_fullStr |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
title_full_unstemmed |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
title_sort |
Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A |
author |
Divsalar,Adeleh |
author_facet |
Divsalar,Adeleh Saboury,Ali Akbar Ahmad,Faizan Moosavi-Movahedi,Ali Akbar |
author_role |
author |
author2 |
Saboury,Ali Akbar Ahmad,Faizan Moosavi-Movahedi,Ali Akbar |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Divsalar,Adeleh Saboury,Ali Akbar Ahmad,Faizan Moosavi-Movahedi,Ali Akbar |
dc.subject.por.fl_str_mv |
β-lactoglobulin temperature Cr(III) ions tertiary structure Tm value |
topic |
β-lactoglobulin temperature Cr(III) ions tertiary structure Tm value |
description |
Thermodynamic studies of the effect of temperature (27-47 ºC) on the structure of bovine b-lactoglobulin-A (BLG-A) in the absence and presence of Cr(III) containing 50 mmol L-1 sodium chloride have been carried out using UV-Visible absorption spectroscopy, far and near circular dichroism (CD) and fluorescence spectroscopy. The far-UV CD studies do not show any significant change in the secondary structure of the protein at different temperatures in the absence and presence of Cr(III). On the contrary, the near-UV CD studies show change in the tertiary structure of the native BLG on increasing the temperature, indicating the exposure of Tyr residues. Fluorescence spectroscopic studies on the native BLG-A in the absence and presence of Cr(III) represent considerable change in the tertiary structure of the protein due to the increase in temperature. Due to protein stabilization in the presence of Cr(III) ions, the tertiary structure of BLG represents considerable alterations at 37 and 47 ο C that is in agreement with increasing of Tm values at these temperatures. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532009001000003 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532009001000003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50532009001000003 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.20 n.10 2009 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318170287112192 |