An improved method to measure all rate constants in the simplest enzyme kinetics model
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Publication:427459
DOI10.1007/S10910-011-9922-4zbMATH Open1318.92016OpenAlexW2047048865MaRDI QIDQ427459FDOQ427459
Authors: Yuefeng Shen, Bo Li, Bang-He Li
Publication date: 13 June 2012
Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s10910-011-9922-4
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Cites Work
- Enzyme kinetics at high enzyme concentration
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
- Dynamical models in biology
- On the validity of the steady state assumption of enzyme kinetics
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- Title not available (Why is that?)
Cited In (7)
- Determination of hammerhead ribozyme kinetic constants at high molar ratio ribozyme-substrate
- Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
- A method for writing enzyme rate equations: Application to the estimation of the number and size of key proton families
- A novel approach to measure all rate constants in the simplest enzyme kinetics model
- Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements
- A much better replacement of the Michaelis-Menten equation and its application
- Metabolic rate constants: some computational aspects
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