Schnell, S. and Maini, P. K. (2002) Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations. Mathematical and Computer Modelling, 35 (1-2). pp. 137-144.
Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed.
|Uncontrolled Keywords:||Total quasi-steady-state approximation; Fitting procedure; Aggregation technique; Singular perturbation|
|Subjects:||A - C > Biology and other natural sciences|
|Research Groups:||Centre for Mathematical Biology|
|Deposited By:||Philip Maini|
|Deposited On:||20 Nov 2006|
|Last Modified:||29 May 2015 18:21|
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