Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
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Publication:1708501
DOI10.1007/s10910-017-0791-3zbMath1385.92024OpenAlexW2952255773WikidataQ59306606 ScholiaQ59306606MaRDI QIDQ1708501
Publication date: 23 March 2018
Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s10910-017-0791-3
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Cites Work
- Unnamed Item
- Michaelis-Menten kinetics at high enzyme concentrations
- On the appropriate use of asymptotic expansions in enzyme kinetics
- A perturbation solution of Michaelis-Menten kinetics in a ``total framework
- Enzyme kinetics at high enzyme concentration
- On the validity of the steady state assumption of enzyme kinetics
- Design and analysis of computer experiments. With comments and a rejoinder by the authors
- Mathematical biology. Vol. 1: An introduction.
- Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
- On the Lambert \(w\) function
- Extending the quasi-steady state approximation by changing variables
- Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant
- A simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total framework
- Invariant manifold methods for metabolic model reduction
- An Algorithm for Least-Squares Estimation of Nonlinear Parameters
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
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