Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes

Autores
Rigos, Carolina Fortes; de Lima Santos, Hérica; Yoneda, Juliana Sakamoto; Montich, Guillermo Gabriel; Maggio, Bruno; Ciancaglini, Pietro
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We studied the thermal dependence of amide I′ infrared absorption and fluorescence emission of Trp residues in the Na,K-ATPase of rabbit kidney. We studied the whole enzyme solubilized with detergent, the whole enzyme reconstituted in proteoliposomes and the protein fraction that remained in the lipid membrane after the trypsin digestion of the proteoliposomes. Cooperative unfolding and aggregation with increasing temperature were observed in the whole protein, whether solubilized or reconstituted, but not in the fraction remaining after trypsinization. The protein influenced the physical state of the lipid, decreasing the temperature of the gel to liquid-crystalline phase transition and the degree of cooperativity. This study provides new information for the understanding of the processes controlling the association mechanisms that are important for enzyme function in natural membranes. © 2009 Elsevier B.V. All rights reserved.
Fil: Rigos, Carolina Fortes. Universidade de Sao Paulo; Brasil
Fil: de Lima Santos, Hérica. Universidade Federal de Sao Joao Del-rei; Brasil
Fil: Yoneda, Juliana Sakamoto. Universidade de Sao Paulo; Brasil
Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Ciancaglini, Pietro. Universidade de Sao Paulo; Brasil
Materia
DETERGENT SOLUBILIZED
FTIR
NA,K-ATPASE
PROTEOLIPOSOMES RECONSTITUTED
THERMAL AGGREGATION
TRP EMISSION
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:11336/186599
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/186599
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomesRigos, Carolina Fortesde Lima Santos, HéricaYoneda, Juliana SakamotoMontich, Guillermo GabrielMaggio, BrunoCiancaglini, PietroDETERGENT SOLUBILIZEDFTIRNA,K-ATPASEPROTEOLIPOSOMES RECONSTITUTEDTHERMAL AGGREGATIONTRP EMISSIONhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1We studied the thermal dependence of amide I′ infrared absorption and fluorescence emission of Trp residues in the Na,K-ATPase of rabbit kidney. We studied the whole enzyme solubilized with detergent, the whole enzyme reconstituted in proteoliposomes and the protein fraction that remained in the lipid membrane after the trypsin digestion of the proteoliposomes. Cooperative unfolding and aggregation with increasing temperature were observed in the whole protein, whether solubilized or reconstituted, but not in the fraction remaining after trypsinization. The protein influenced the physical state of the lipid, decreasing the temperature of the gel to liquid-crystalline phase transition and the degree of cooperativity. This study provides new information for the understanding of the processes controlling the association mechanisms that are important for enzyme function in natural membranes. © 2009 Elsevier B.V. All rights reserved.Fil: Rigos, Carolina Fortes. Universidade de Sao Paulo; BrasilFil: de Lima Santos, Hérica. Universidade Federal de Sao Joao Del-rei; BrasilFil: Yoneda, Juliana Sakamoto. Universidade de Sao Paulo; BrasilFil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Ciancaglini, Pietro. Universidade de Sao Paulo; BrasilElsevier Science2010-01info: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/11336/186599Rigos, Carolina Fortes; de Lima Santos, Hérica; Yoneda, Juliana Sakamoto; Montich, Guillermo Gabriel; Maggio, Bruno; et al.; Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes; Elsevier Science; Biophysical Chemistry; 146; 1; 1-2010; 36-410301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2009.10.002info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0301462209002038?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:51:20Zoai:ri.conicet.gov.ar:11336/186599instacron: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:34982025-09-29 09:51:21.018CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
title Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
spellingShingle Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
Rigos, Carolina Fortes
DETERGENT SOLUBILIZED
FTIR
NA,K-ATPASE
PROTEOLIPOSOMES RECONSTITUTED
THERMAL AGGREGATION
TRP EMISSION
title_short Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
title_full Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
title_fullStr Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
title_full_unstemmed Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
title_sort Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes
dc.creator.none.fl_str_mv Rigos, Carolina Fortes
de Lima Santos, Hérica
Yoneda, Juliana Sakamoto
Montich, Guillermo Gabriel
Maggio, Bruno
Ciancaglini, Pietro
author Rigos, Carolina Fortes
author_facet Rigos, Carolina Fortes
de Lima Santos, Hérica
Yoneda, Juliana Sakamoto
Montich, Guillermo Gabriel
Maggio, Bruno
Ciancaglini, Pietro
author_role author
author2 de Lima Santos, Hérica
Yoneda, Juliana Sakamoto
Montich, Guillermo Gabriel
Maggio, Bruno
Ciancaglini, Pietro
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv DETERGENT SOLUBILIZED
FTIR
NA,K-ATPASE
PROTEOLIPOSOMES RECONSTITUTED
THERMAL AGGREGATION
TRP EMISSION
topic DETERGENT SOLUBILIZED
FTIR
NA,K-ATPASE
PROTEOLIPOSOMES RECONSTITUTED
THERMAL AGGREGATION
TRP EMISSION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We studied the thermal dependence of amide I′ infrared absorption and fluorescence emission of Trp residues in the Na,K-ATPase of rabbit kidney. We studied the whole enzyme solubilized with detergent, the whole enzyme reconstituted in proteoliposomes and the protein fraction that remained in the lipid membrane after the trypsin digestion of the proteoliposomes. Cooperative unfolding and aggregation with increasing temperature were observed in the whole protein, whether solubilized or reconstituted, but not in the fraction remaining after trypsinization. The protein influenced the physical state of the lipid, decreasing the temperature of the gel to liquid-crystalline phase transition and the degree of cooperativity. This study provides new information for the understanding of the processes controlling the association mechanisms that are important for enzyme function in natural membranes. © 2009 Elsevier B.V. All rights reserved.
Fil: Rigos, Carolina Fortes. Universidade de Sao Paulo; Brasil
Fil: de Lima Santos, Hérica. Universidade Federal de Sao Joao Del-rei; Brasil
Fil: Yoneda, Juliana Sakamoto. Universidade de Sao Paulo; Brasil
Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Ciancaglini, Pietro. Universidade de Sao Paulo; Brasil
description We studied the thermal dependence of amide I′ infrared absorption and fluorescence emission of Trp residues in the Na,K-ATPase of rabbit kidney. We studied the whole enzyme solubilized with detergent, the whole enzyme reconstituted in proteoliposomes and the protein fraction that remained in the lipid membrane after the trypsin digestion of the proteoliposomes. Cooperative unfolding and aggregation with increasing temperature were observed in the whole protein, whether solubilized or reconstituted, but not in the fraction remaining after trypsinization. The protein influenced the physical state of the lipid, decreasing the temperature of the gel to liquid-crystalline phase transition and the degree of cooperativity. This study provides new information for the understanding of the processes controlling the association mechanisms that are important for enzyme function in natural membranes. © 2009 Elsevier B.V. All rights reserved.
publishDate 2010
dc.date.none.fl_str_mv 2010-01
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/11336/186599
Rigos, Carolina Fortes; de Lima Santos, Hérica; Yoneda, Juliana Sakamoto; Montich, Guillermo Gabriel; Maggio, Bruno; et al.; Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes; Elsevier Science; Biophysical Chemistry; 146; 1; 1-2010; 36-41
0301-4622
CONICET Digital
CONICET
url http://hdl.handle.net/11336/186599
identifier_str_mv Rigos, Carolina Fortes; de Lima Santos, Hérica; Yoneda, Juliana Sakamoto; Montich, Guillermo Gabriel; Maggio, Bruno; et al.; Cytoplasmatic domain of Na,K-ATPase α-subunit is responsible for the aggregation of the enzyme in proteoliposomes; Elsevier Science; Biophysical Chemistry; 146; 1; 1-2010; 36-41
0301-4622
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2009.10.002
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0301462209002038?via%3Dihub
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
publisher.none.fl_str_mv Elsevier Science
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
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score 13.070432

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