Effects of temperature and chromium (III) ion on the structure of bovine β-Lactoglobulin-A

Detalhes bibliográficos
Autor(a) principal: Divsalar,Adeleh
Data de Publicação: 2009
Outros Autores: Saboury,Ali Akbar, Ahmad,Faizan, Moosavi-Movahedi,Ali Akbar
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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spelling 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
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