The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route
Occlusion of K+ or its congeners in the Na+/K+-ATPase occurs after K+-dependent dephosphorylation (physiological route) or in media lacking ATP and Na+ (direct route). The effects of Pi or ATP on the kinetics of deocclusion of the K+-congener Rb+ formed by each of the above mentioned routes was inde...
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todo:paper_00219258_v277_n8_p5910_GonzalezLebrero2023-10-03T14:23:02Z The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route González-Lebrero, R.M. Kaufman, S.B. Montes, M.R. Nørby, J.G. Garrahan, P.J. Rossi, R.C. Physiology Positive ions Potassium Rate constants Rubidium Sodium Congeners Enzymes adenosine triphosphatase (potassium sodium) adenosine triphosphate phosphate potassium ion rubidium ion sodium ion active transport article dephosphorylation enzyme analysis hydrolysis nonhuman priority journal swine Adenosine Triphosphate Animals Kidney Kinetics Models, Theoretical Na(+)-K(+)-Exchanging ATPase Phosphates Regression Analysis Rubidium Swine Sus scrofa Occlusion of K+ or its congeners in the Na+/K+-ATPase occurs after K+-dependent dephosphorylation (physiological route) or in media lacking ATP and Na+ (direct route). The effects of Pi or ATP on the kinetics of deocclusion of the K+-congener Rb+ formed by each of the above mentioned routes was independent of the route of occlusion, which suggests that both routes lead to the same enzyme intermediate. The time course of occlusion via the direct route can be described by the sum of two exponential functions plus a small component of very high velocity. At equilibrium, occluded Rb+ is a hyperbolic function of free [Rb+] suggesting that the direct route results in enzyme states holding either one or two occluded Rb+. Release of occluded Rb+ follows the sum of two decreasing exponential functions of time, corresponding to two phases with similar sizes. These phases are not caused by independent physical compartments. The rate constant of one of the phases is reduced up to 30 times by free Rb+. When Rb+ is the only pump ligand, the kinetics of occlusion and deocclusion through the direct route are consistent with an ordered-sequential process with additional independent step(s) interposed between the uptake or the release of each occluded Rb+. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219258_v277_n8_p5910_GonzalezLebrero |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Physiology Positive ions Potassium Rate constants Rubidium Sodium Congeners Enzymes adenosine triphosphatase (potassium sodium) adenosine triphosphate phosphate potassium ion rubidium ion sodium ion active transport article dephosphorylation enzyme analysis hydrolysis nonhuman priority journal swine Adenosine Triphosphate Animals Kidney Kinetics Models, Theoretical Na(+)-K(+)-Exchanging ATPase Phosphates Regression Analysis Rubidium Swine Sus scrofa |
| spellingShingle |
Physiology Positive ions Potassium Rate constants Rubidium Sodium Congeners Enzymes adenosine triphosphatase (potassium sodium) adenosine triphosphate phosphate potassium ion rubidium ion sodium ion active transport article dephosphorylation enzyme analysis hydrolysis nonhuman priority journal swine Adenosine Triphosphate Animals Kidney Kinetics Models, Theoretical Na(+)-K(+)-Exchanging ATPase Phosphates Regression Analysis Rubidium Swine Sus scrofa González-Lebrero, R.M. Kaufman, S.B. Montes, M.R. Nørby, J.G. Garrahan, P.J. Rossi, R.C. The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| topic_facet |
Physiology Positive ions Potassium Rate constants Rubidium Sodium Congeners Enzymes adenosine triphosphatase (potassium sodium) adenosine triphosphate phosphate potassium ion rubidium ion sodium ion active transport article dephosphorylation enzyme analysis hydrolysis nonhuman priority journal swine Adenosine Triphosphate Animals Kidney Kinetics Models, Theoretical Na(+)-K(+)-Exchanging ATPase Phosphates Regression Analysis Rubidium Swine Sus scrofa |
| description |
Occlusion of K+ or its congeners in the Na+/K+-ATPase occurs after K+-dependent dephosphorylation (physiological route) or in media lacking ATP and Na+ (direct route). The effects of Pi or ATP on the kinetics of deocclusion of the K+-congener Rb+ formed by each of the above mentioned routes was independent of the route of occlusion, which suggests that both routes lead to the same enzyme intermediate. The time course of occlusion via the direct route can be described by the sum of two exponential functions plus a small component of very high velocity. At equilibrium, occluded Rb+ is a hyperbolic function of free [Rb+] suggesting that the direct route results in enzyme states holding either one or two occluded Rb+. Release of occluded Rb+ follows the sum of two decreasing exponential functions of time, corresponding to two phases with similar sizes. These phases are not caused by independent physical compartments. The rate constant of one of the phases is reduced up to 30 times by free Rb+. When Rb+ is the only pump ligand, the kinetics of occlusion and deocclusion through the direct route are consistent with an ordered-sequential process with additional independent step(s) interposed between the uptake or the release of each occluded Rb+. |
| format |
JOUR |
| author |
González-Lebrero, R.M. Kaufman, S.B. Montes, M.R. Nørby, J.G. Garrahan, P.J. Rossi, R.C. |
| author_facet |
González-Lebrero, R.M. Kaufman, S.B. Montes, M.R. Nørby, J.G. Garrahan, P.J. Rossi, R.C. |
| author_sort |
González-Lebrero, R.M. |
| title |
The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| title_short |
The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| title_full |
The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| title_fullStr |
The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| title_full_unstemmed |
The occlusion of Rb+ in the Na+/K+-ATPase. I. The identity of occluded states formed by the physiological or the direct routes: Occlusion/deocclusion kinetics through the direct route |
| title_sort |
occlusion of rb+ in the na+/k+-atpase. i. the identity of occluded states formed by the physiological or the direct routes: occlusion/deocclusion kinetics through the direct route |
| url |
http://hdl.handle.net/20.500.12110/paper_00219258_v277_n8_p5910_GonzalezLebrero |
| work_keys_str_mv |
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