The total quasi-steady-state approximation for fully competitive enzyme reactions
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Publication:2426260
DOI10.1007/s11538-006-9136-2zbMath1133.92323WikidataQ51937391 ScholiaQ51937391MaRDI QIDQ2426260
Alberto Maria Bersani, Morten Gram Pedersen, Enrico Bersani
Publication date: 22 April 2008
Published in: Bulletin of Mathematical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s11538-006-9136-2
Michaelis-Menten kinetics; QSSA; quasi-steady-state assumption; competitive substrates; substrate-inhibitor system
37N25: Dynamical systems in biology
92C45: Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.)
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Cites Work
- Michaelis-Menten kinetics at high enzyme concentrations
- Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
- Time-dependent closed form solutions for fully competitive enzyme reactions
- Enzyme kinetics at high enzyme concentration
- On the validity of the steady state assumption of enzyme kinetics
- Extending the quasi-steady state approximation by changing variables
- Stochastic approaches for modelling in vivo reactions
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
