Monotonicity properties of the Michaelis-Menten reactions of enzyme kinetics

DOI10.1216/RMJM/1181073068MaRDI QIDQ2639795zbMATH OpenOpenAlexFDO

Authors 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 kineticsinitial concentrationmass-action kineticsMichaelis-Menten reactionsmonotonicity propertiessigns of the derivatives of the concentrations

Mathematics Subject Classification ID

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

Recommendations

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Cites work

• scientific article; zbMATH DE number 4125848 (Why is no real title available?)
• scientific article; zbMATH DE number 3440822 (Why is no real title available?)
• scientific article; zbMATH DE number 3448490 (Why is no real title available?)
• scientific article; zbMATH DE number 3109695 (Why is no real title available?)
• Systems of Ordinary Differential Equations Which Generate an Order Preserving Flow. A Survey of Results
• The dynamical systems approach to differential equations

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• Monotonicity properties of chemical reactions with a single initial bimolecular step
• 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
• Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades
• Michaelis-Menten kinetics at high enzyme concentrations
• scientific article; zbMATH DE number 1100549 (Why is no real title available?)
• Monotonicity with respect to closed convex cones II

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