Studies on the differential equations of enzyme kinetics. I. Bimolecular scheme: simplified model

DOI10.1155/S0161171287000887MaRDI QIDQ1107466zbMATH OpenOpenAlexFDO

Authors Claude Marmasse, Joseph Wiener

Publication date 1987

Published in International Journal of Mathematics and Mathematical Sciences (Search for Journal in Brave)

Full work available at URL https://eudml.org/doc/46300

zbMATH Keywords

biochemistryenzyme kineticsisoclinesrapid equilibrium theorysteady-state approximation

Mathematics Subject Classification ID

Theoretical approximation of solutions to ordinary differential equations (34A45) Topological structure of integral curves, singular points, limit cycles of ordinary differential equations (34C05) Chemical kinetics in thermodynamics and heat transfer (80A30) Physiological, cellular and medical topics (92Cxx)

Review text

Summary: The main properties of the solution of the differential system of the model are obtained by qualitative integration. The integral curve is compared with the solutions given by the two classical approximations to the problem: it is shown that the steady-state approximation is to be preferred to the rapid equilibrium theory as a general method and the conditions under which they will furnish accurate results are discussed.

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(5)

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• Modeling and numerical simulation of biotin carboxylase kinetics: implications for half-sites reactivity
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• A comparative analysis of strict kinetic equations for the enzyme systems and equations obtained by the rapid equilibrium approach
• Qualitative investigation of dynamical equation system of hemoglobin (or allosteric enzymes)

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