Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+

Autores
Monti, José Luis Eugenio; Rossi, Rolando Carlos; Montes, Monica Raquel
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A comprehensive study of the interaction between Na+ and K+ with the Na+/K+-ATPase requires dissecting the incidence of alternative cycling modes on activity measurements in which one or both of these cations are absent. With this aim, we used membrane fragments containing pig-kidney Na+/K+-ATPase to perform measurements, at 25ºC and pH=7.4, of ATPase activity and steady state levels of (i) intermediates containing occluded Rb+ at different [Rb+] in media lacking Na+, and (ii) phosphorylated intermediates at different [Na+] in media lacking Rb+. Most relevant results are: (1) Rb+ can be occluded through an ATPasic cycling mode that takes place in the absence of Na+ ions, (2) the kinetic behavior of the phosphoenzyme formed by ATP in the absence of Na+ is different from the one that is formed with Na+, and (3) binding of Na+ to transport sites during catalysis is not at random unless rapid equilibrium holds.
Fil: Monti, José Luis Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Rossi, Rolando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Montes, Monica Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
Materia
Na+/K+-Atpase
Steady-State Kinetics
Phosphoenzyme
Rb+-Occlusion
Atpase Activity
Minimal Model
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/4524
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/4524
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+Monti, José Luis EugenioRossi, Rolando CarlosMontes, Monica RaquelNa+/K+-AtpaseSteady-State KineticsPhosphoenzymeRb+-OcclusionAtpase ActivityMinimal Modelhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A comprehensive study of the interaction between Na+ and K+ with the Na+/K+-ATPase requires dissecting the incidence of alternative cycling modes on activity measurements in which one or both of these cations are absent. With this aim, we used membrane fragments containing pig-kidney Na+/K+-ATPase to perform measurements, at 25ºC and pH=7.4, of ATPase activity and steady state levels of (i) intermediates containing occluded Rb+ at different [Rb+] in media lacking Na+, and (ii) phosphorylated intermediates at different [Na+] in media lacking Rb+. Most relevant results are: (1) Rb+ can be occluded through an ATPasic cycling mode that takes place in the absence of Na+ ions, (2) the kinetic behavior of the phosphoenzyme formed by ATP in the absence of Na+ is different from the one that is formed with Na+, and (3) binding of Na+ to transport sites during catalysis is not at random unless rapid equilibrium holds.Fil: Monti, José Luis Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; ArgentinaFil: Rossi, Rolando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; ArgentinaFil: Montes, Monica Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; ArgentinaElsevier2013-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/mswordhttp://hdl.handle.net/11336/4524Monti, José Luis Eugenio; Rossi, Rolando Carlos; Montes, Monica Raquel; Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+; Elsevier; Biochimica And Biophysica Acta; 1828; 5; 5-2013; 1374-13830006-3002enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613000229info:eu-repo/semantics/altIdentifier/issn/0006-3002info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.01.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:00Zoai:ri.conicet.gov.ar:11336/4524instacron: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 10:01:01.065CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
title Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
spellingShingle Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
Monti, José Luis Eugenio
Na+/K+-Atpase
Steady-State Kinetics
Phosphoenzyme
Rb+-Occlusion
Atpase Activity
Minimal Model
title_short Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
title_full Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
title_fullStr Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
title_full_unstemmed Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
title_sort Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
dc.creator.none.fl_str_mv Monti, José Luis Eugenio
Rossi, Rolando Carlos
Montes, Monica Raquel
author Monti, José Luis Eugenio
author_facet Monti, José Luis Eugenio
Rossi, Rolando Carlos
Montes, Monica Raquel
author_role author
author2 Rossi, Rolando Carlos
Montes, Monica Raquel
author2_role author
author
dc.subject.none.fl_str_mv Na+/K+-Atpase
Steady-State Kinetics
Phosphoenzyme
Rb+-Occlusion
Atpase Activity
Minimal Model
topic Na+/K+-Atpase
Steady-State Kinetics
Phosphoenzyme
Rb+-Occlusion
Atpase Activity
Minimal Model
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A comprehensive study of the interaction between Na+ and K+ with the Na+/K+-ATPase requires dissecting the incidence of alternative cycling modes on activity measurements in which one or both of these cations are absent. With this aim, we used membrane fragments containing pig-kidney Na+/K+-ATPase to perform measurements, at 25ºC and pH=7.4, of ATPase activity and steady state levels of (i) intermediates containing occluded Rb+ at different [Rb+] in media lacking Na+, and (ii) phosphorylated intermediates at different [Na+] in media lacking Rb+. Most relevant results are: (1) Rb+ can be occluded through an ATPasic cycling mode that takes place in the absence of Na+ ions, (2) the kinetic behavior of the phosphoenzyme formed by ATP in the absence of Na+ is different from the one that is formed with Na+, and (3) binding of Na+ to transport sites during catalysis is not at random unless rapid equilibrium holds.
Fil: Monti, José Luis Eugenio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Rossi, Rolando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
Fil: Montes, Monica Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Fisicoquímica Biológicas; Argentina
description A comprehensive study of the interaction between Na+ and K+ with the Na+/K+-ATPase requires dissecting the incidence of alternative cycling modes on activity measurements in which one or both of these cations are absent. With this aim, we used membrane fragments containing pig-kidney Na+/K+-ATPase to perform measurements, at 25ºC and pH=7.4, of ATPase activity and steady state levels of (i) intermediates containing occluded Rb+ at different [Rb+] in media lacking Na+, and (ii) phosphorylated intermediates at different [Na+] in media lacking Rb+. Most relevant results are: (1) Rb+ can be occluded through an ATPasic cycling mode that takes place in the absence of Na+ ions, (2) the kinetic behavior of the phosphoenzyme formed by ATP in the absence of Na+ is different from the one that is formed with Na+, and (3) binding of Na+ to transport sites during catalysis is not at random unless rapid equilibrium holds.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/4524
Monti, José Luis Eugenio; Rossi, Rolando Carlos; Montes, Monica Raquel; Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+; Elsevier; Biochimica And Biophysica Acta; 1828; 5; 5-2013; 1374-1383
0006-3002
url http://hdl.handle.net/11336/4524
identifier_str_mv Monti, José Luis Eugenio; Rossi, Rolando Carlos; Montes, Monica Raquel; Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+; Elsevier; Biochimica And Biophysica Acta; 1828; 5; 5-2013; 1374-1383
0006-3002
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613000229
info:eu-repo/semantics/altIdentifier/issn/0006-3002
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.01.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/msword
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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_ 1844613798255656960
score 13.070432

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