Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+
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...
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2013
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1828_n5_p1374_Monti http://hdl.handle.net/20.500.12110/paper_00052736_v1828_n5_p1374_Monti |
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paper:paper_00052736_v1828_n5_p1374_Monti2023-06-08T14:29:51Z Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+ ATPase activity Minimal model Na+/K+-ATPase Phosphoenzyme Rb+-occlusion Steady-state kinetics adenosine triphosphatase (potassium sodium) adenosine triphosphate rubidium sodium ion article enzyme activity enzyme binding enzyme mechanism enzyme metabolism enzyme phosphorylation molecular interaction pH potassium transport priority journal process model sodium transport steady state temperature sensitivity transport kinetics Adenosine Diphosphate Adenosine Triphosphate Animals Biocatalysis Dose-Response Relationship, Drug Kidney Medulla Kinetics Models, Biological Phosphorylation Protein Binding Rubidium Sodium Sodium-Potassium-Exchanging ATPase Swine 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 25 C 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. © 2013 Elsevier B.V. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1828_n5_p1374_Monti http://hdl.handle.net/20.500.12110/paper_00052736_v1828_n5_p1374_Monti |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ATPase activity Minimal model Na+/K+-ATPase Phosphoenzyme Rb+-occlusion Steady-state kinetics adenosine triphosphatase (potassium sodium) adenosine triphosphate rubidium sodium ion article enzyme activity enzyme binding enzyme mechanism enzyme metabolism enzyme phosphorylation molecular interaction pH potassium transport priority journal process model sodium transport steady state temperature sensitivity transport kinetics Adenosine Diphosphate Adenosine Triphosphate Animals Biocatalysis Dose-Response Relationship, Drug Kidney Medulla Kinetics Models, Biological Phosphorylation Protein Binding Rubidium Sodium Sodium-Potassium-Exchanging ATPase Swine |
| spellingShingle |
ATPase activity Minimal model Na+/K+-ATPase Phosphoenzyme Rb+-occlusion Steady-state kinetics adenosine triphosphatase (potassium sodium) adenosine triphosphate rubidium sodium ion article enzyme activity enzyme binding enzyme mechanism enzyme metabolism enzyme phosphorylation molecular interaction pH potassium transport priority journal process model sodium transport steady state temperature sensitivity transport kinetics Adenosine Diphosphate Adenosine Triphosphate Animals Biocatalysis Dose-Response Relationship, Drug Kidney Medulla Kinetics Models, Biological Phosphorylation Protein Binding Rubidium Sodium Sodium-Potassium-Exchanging ATPase Swine Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+ |
| topic_facet |
ATPase activity Minimal model Na+/K+-ATPase Phosphoenzyme Rb+-occlusion Steady-state kinetics adenosine triphosphatase (potassium sodium) adenosine triphosphate rubidium sodium ion article enzyme activity enzyme binding enzyme mechanism enzyme metabolism enzyme phosphorylation molecular interaction pH potassium transport priority journal process model sodium transport steady state temperature sensitivity transport kinetics Adenosine Diphosphate Adenosine Triphosphate Animals Biocatalysis Dose-Response Relationship, Drug Kidney Medulla Kinetics Models, Biological Phosphorylation Protein Binding Rubidium Sodium Sodium-Potassium-Exchanging ATPase Swine |
| 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 25 C 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. © 2013 Elsevier B.V. |
| title |
Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+ |
| 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+ |
| publishDate |
2013 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1828_n5_p1374_Monti http://hdl.handle.net/20.500.12110/paper_00052736_v1828_n5_p1374_Monti |
| _version_ |
1768545445440651264 |