A fluorescence study of human serum albumin binding sites modification by hypochlorite

Autores
Lissi, Eduardo; Biasutti, Maria Alicia; Abuin, Elsa; León, Luis
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A study has been made on the properties of human serum albumin (HSA) binding sites and how they are modified by pre-oxidation of the protein with hypochlorite. The oxidation extent was assessed from changes in the protein intrinsic fluorescence and production of carbonyl groups. HSA retains its solute binding capacity even after exposure to relatively large amounts of hypochlorite (up to 40 oxidant molecules per protein). From an analysis of the binding isotherms of dansyl sarcosine (DS) and dansyl-1-sulfonamide (DNSA) to native and hypochlorite treated albumin it is concluded that pre-oxidation of the protein reduces the number of active sites without affecting the binding capacity of the remaining binding sites. From DS and DNSA fluorescence anisotropy, Laurdan anisotropy and generalized polarization measurements, it is concluded that both Sites I and II in the native protein provide very rigid environments to the bound probes. These characteristics of the sites remain even after extensive treatment with hypochlorite. This stubbornness of HSA could allow the protein to maintain its function along its in vivo lifetime.
Fil: Lissi, Eduardo. Universidad de Santiago de Chile; Chile
Fil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Abuin, Elsa. Universidad de Santiago de Chile; Chile
Fil: León, Luis. Universidad de Santiago de Chile; Chile
Materia
Human serum albumin
Hypochlorite
Dansyl derivatives
Prodan
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/240760
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A fluorescence study of human serum albumin binding sites modification by hypochloriteLissi, EduardoBiasutti, Maria AliciaAbuin, ElsaLeón, LuisHuman serum albuminHypochloriteDansyl derivativesProdanhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A study has been made on the properties of human serum albumin (HSA) binding sites and how they are modified by pre-oxidation of the protein with hypochlorite. The oxidation extent was assessed from changes in the protein intrinsic fluorescence and production of carbonyl groups. HSA retains its solute binding capacity even after exposure to relatively large amounts of hypochlorite (up to 40 oxidant molecules per protein). From an analysis of the binding isotherms of dansyl sarcosine (DS) and dansyl-1-sulfonamide (DNSA) to native and hypochlorite treated albumin it is concluded that pre-oxidation of the protein reduces the number of active sites without affecting the binding capacity of the remaining binding sites. From DS and DNSA fluorescence anisotropy, Laurdan anisotropy and generalized polarization measurements, it is concluded that both Sites I and II in the native protein provide very rigid environments to the bound probes. These characteristics of the sites remain even after extensive treatment with hypochlorite. This stubbornness of HSA could allow the protein to maintain its function along its in vivo lifetime.Fil: Lissi, Eduardo. Universidad de Santiago de Chile; ChileFil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Abuin, Elsa. Universidad de Santiago de Chile; ChileFil: León, Luis. Universidad de Santiago de Chile; ChileElsevier Science SA2009-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/240760Lissi, Eduardo; Biasutti, Maria Alicia; Abuin, Elsa; León, Luis; A fluorescence study of human serum albumin binding sites modification by hypochlorite; Elsevier Science SA; Journal of Photochemistry and Photobiology B: Biology; 94; 2; 6-2009; 77-811011-1344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134408002066info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphotobiol.2008.10.007info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:07:21Zoai:ri.conicet.gov.ar:11336/240760instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:07:21.628CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A fluorescence study of human serum albumin binding sites modification by hypochlorite
title A fluorescence study of human serum albumin binding sites modification by hypochlorite
spellingShingle A fluorescence study of human serum albumin binding sites modification by hypochlorite
Lissi, Eduardo
Human serum albumin
Hypochlorite
Dansyl derivatives
Prodan
title_short A fluorescence study of human serum albumin binding sites modification by hypochlorite
title_full A fluorescence study of human serum albumin binding sites modification by hypochlorite
title_fullStr A fluorescence study of human serum albumin binding sites modification by hypochlorite
title_full_unstemmed A fluorescence study of human serum albumin binding sites modification by hypochlorite
title_sort A fluorescence study of human serum albumin binding sites modification by hypochlorite
dc.creator.none.fl_str_mv Lissi, Eduardo
Biasutti, Maria Alicia
Abuin, Elsa
León, Luis
author Lissi, Eduardo
author_facet Lissi, Eduardo
Biasutti, Maria Alicia
Abuin, Elsa
León, Luis
author_role author
author2 Biasutti, Maria Alicia
Abuin, Elsa
León, Luis
author2_role author
author
author
dc.subject.none.fl_str_mv Human serum albumin
Hypochlorite
Dansyl derivatives
Prodan
topic Human serum albumin
Hypochlorite
Dansyl derivatives
Prodan
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A study has been made on the properties of human serum albumin (HSA) binding sites and how they are modified by pre-oxidation of the protein with hypochlorite. The oxidation extent was assessed from changes in the protein intrinsic fluorescence and production of carbonyl groups. HSA retains its solute binding capacity even after exposure to relatively large amounts of hypochlorite (up to 40 oxidant molecules per protein). From an analysis of the binding isotherms of dansyl sarcosine (DS) and dansyl-1-sulfonamide (DNSA) to native and hypochlorite treated albumin it is concluded that pre-oxidation of the protein reduces the number of active sites without affecting the binding capacity of the remaining binding sites. From DS and DNSA fluorescence anisotropy, Laurdan anisotropy and generalized polarization measurements, it is concluded that both Sites I and II in the native protein provide very rigid environments to the bound probes. These characteristics of the sites remain even after extensive treatment with hypochlorite. This stubbornness of HSA could allow the protein to maintain its function along its in vivo lifetime.
Fil: Lissi, Eduardo. Universidad de Santiago de Chile; Chile
Fil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Abuin, Elsa. Universidad de Santiago de Chile; Chile
Fil: León, Luis. Universidad de Santiago de Chile; Chile
description A study has been made on the properties of human serum albumin (HSA) binding sites and how they are modified by pre-oxidation of the protein with hypochlorite. The oxidation extent was assessed from changes in the protein intrinsic fluorescence and production of carbonyl groups. HSA retains its solute binding capacity even after exposure to relatively large amounts of hypochlorite (up to 40 oxidant molecules per protein). From an analysis of the binding isotherms of dansyl sarcosine (DS) and dansyl-1-sulfonamide (DNSA) to native and hypochlorite treated albumin it is concluded that pre-oxidation of the protein reduces the number of active sites without affecting the binding capacity of the remaining binding sites. From DS and DNSA fluorescence anisotropy, Laurdan anisotropy and generalized polarization measurements, it is concluded that both Sites I and II in the native protein provide very rigid environments to the bound probes. These characteristics of the sites remain even after extensive treatment with hypochlorite. This stubbornness of HSA could allow the protein to maintain its function along its in vivo lifetime.
publishDate 2009
dc.date.none.fl_str_mv 2009-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/240760
Lissi, Eduardo; Biasutti, Maria Alicia; Abuin, Elsa; León, Luis; A fluorescence study of human serum albumin binding sites modification by hypochlorite; Elsevier Science SA; Journal of Photochemistry and Photobiology B: Biology; 94; 2; 6-2009; 77-81
1011-1344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/240760
identifier_str_mv Lissi, Eduardo; Biasutti, Maria Alicia; Abuin, Elsa; León, Luis; A fluorescence study of human serum albumin binding sites modification by hypochlorite; Elsevier Science SA; Journal of Photochemistry and Photobiology B: Biology; 94; 2; 6-2009; 77-81
1011-1344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134408002066
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphotobiol.2008.10.007
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science SA
publisher.none.fl_str_mv Elsevier Science SA
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842270000403972096
score 13.13397

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