The Mathematical Institute, University of Oxford, Eprints Archive

Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations

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.

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Abstract

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.

Item Type:Article
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
ID Code:400
Deposited By:Philip Maini
Deposited On:20 Nov 2006
Last Modified:20 Jul 2009 14:21

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