Monotonicity properties of the Michaelis-Menten reactions of enzyme kinetics

DOI10.1216/rmjm/1181073068zbMath0718.92007OpenAlexW2031974008MaRDI QIDQ2639795

David Siegel, D. W. Lozinski

Publication date: 1990

Published in: Rocky Mountain Journal of Mathematics (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1216/rmjm/1181073068

zbMATH Keywords

enzyme kineticsmonotonicity propertiesmass-action kineticsMichaelis-Menten reactionsinitial concentrationsigns of the derivatives of the concentrations

Mathematics Subject Classification ID

Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Qualitative theory for ordinary differential equations (34C99) Chemical kinetics in thermodynamics and heat transfer (80A30) Dynamical systems and ergodic theory (37-XX)

Related Items (3)

Monotonicity of interleukin-1 receptor-ligand binding with respect to antagonist in the presence of decoy receptor ⋮ Quasi-steady state in the Michaelis-Menten system ⋮ Monotonicity with respect to closed convex cones II

Cites Work

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• The dynamical systems approach to differential equations
• Systems of Ordinary Differential Equations Which Generate an Order Preserving Flow. A Survey of Results

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