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Updated: Aug 18, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
Oscillatory activity of P-type membrane adenosine triphosphatases: a kinetic model
B N Goldstein1, A A Mayevsky, D T Zakrjevskaya
1Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. goldstein@iteb.ru
Abstract:
A kinetic model for membrane P-type adenosine triphosphatases is considered, the main application being to the erythrocyte Ca2+-ATPase. It is shown that a simple modification of the known catalytic mechanism of the ATPase by addition of a self-inhibition step and the steady calcium influx leads to damped oscillations in the system discussed. In this way, the model can explain the kinetic experimental results obtained for the purified enzyme in solution as well as for the enzyme incorporated into liposome membranes. The estimated kinetic parameters are close to the experimental ones. Alternative changes in time, demonstrated by the kinetic model for the conformational enzyme states, E(1 )and E(2), confirm the model of two alternatively functioning gates in the ion pumping Ca2+-ATPase.
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