Adenosine triphosphatase kinetics

Post, R.L., Hegyvary, C., Kume, S. (1972). Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540. 

Skubitz KM, Smith TW (1975) Determination of antibody-hapten association kinetics. A simplified experimental approach. J Immunol 114 1369-1374 Smith TW (1972) Ouabain-specific antibodies. Immunochemical properties and reversal of Na,K activated adenosine triphosphatase inhibition. J Clin Invest 51 1583-1593 Smith TW, Harber E (1973) Classical value of the radioimmunoassay of the digitalis glycosides. Pharmacol Rev 25 219-228... 

The activity of ion transport systems, such as sodium- and potassium-activated adenosine triphosphatase, has been studied In vivo by the use of rubidium-87 MRS. This has been possible because rubidium has been shown to substitute for potassium in a number of transmembrane transport systems, accumulating in the intracellular space. Standard in vitro methods of determining Na+/K+-ATPase activity, which also use rubidium, give highly variable measurements and in some cases contradictory results. Many of these problems appear to have been overcome by the use of in vivo Rb MRS, especially when sequential measurements are required. In a longitudinal study of spontaneously hypertensive rats, Rb MRS showed that skeletal muscle rubidium rose at a faster rate in hypertensive rats than in control animals, which is consistent with a marked increase in Na+/K+-ATPase activity. This type of experiment emphasizes the value of in vivo MRS since rubidium kinetics can be determined sequentially on the same animal, minimizing inter/intra-subject variability as well as the number of animals required in the study. 

Ohta S, Tsuboi M, Yoshida M and Kagawa Y (1980) Inter subunit interaction in proton translocating adenosine triphosphatase as revealed by hydrogen exchange kinetics. Biochemistry 19t 2160-2164. Pullman ME and Monroy GC (1963) A naturally occuring inhibitor of mitochondrial adenosine triphosphtase, J. Biol. Chem. 238, 3762-3769. Rott R and Nelson N (1981) Purification and immunological properties of proton ATPase complexes from yeast and rat liver mitochondria, J. Biol. Chem. 256, 9224-9228. 

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