Pages that link to "Item:Q652730"
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The following pages link to Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action (Q652730):
Displaying 26 items.
- Michaelis-Menten kinetics at high enzyme concentrations (Q253479) (← links)
- A Michaelis-Menten-style model for the autocatalytic enzyme prostaglandin H synthase (Q263478) (← links)
- Solving linear unbranched pathways with Michaelis-Menten kinetics using the Lambert \(W\)-function (Q335908) (← links)
- An improved method to measure all rate constants in the simplest enzyme kinetics model (Q427459) (← links)
- Applying structural transition theory to describe enzyme kinetics in heterogeneous systems (Q460904) (← links)
- An alternative analysis of enzyme systems based on the whole reaction time: evaluation of the kinetic parameters and initial enzyme concentration (Q551849) (← links)
- An approximate solution for the transient kinetic behavior of enzyme- catalyzed reactions: The irreversible Michaelis-Menten kinetics (Q580222) (← links)
- A novel approach to measure all rate constants in the simplest enzyme kinetics model (Q1028043) (← links)
- How to derive flux control coefficients from the rate equations of classical enzyme kinetics (Q1126367) (← links)
- A four-proton-families model for pH-dependent enzyme activation: Application to intestinal brush border sucrase (Q1194458) (← links)
- Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis (Q1343388) (← links)
- Mass transport with enzyme reactions (Q1384760) (← links)
- Michaelis-Menten equation for degradation of insoluble substrate (Q1698530) (← links)
- Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions (Q1708501) (← links)
- Perturbation theory in the catalytic rate constant of the Henri-Michaelis-Menten enzymatic reaction (Q1936696) (← links)
- Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation (Q1936971) (← links)
- Impact of enzyme turnover on the dynamics of the Michaelis-Menten model (Q2137774) (← links)
- Interpretation of \(V/K\) isotope effects for enzymatic reactions exhibiting multiple isotopically sensitive steps (Q2202387) (← links)
- General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps (Q2328428) (← links)
- A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails (Q2328450) (← links)
- A further step in the kinetic characterisation of the tyrosinase enzymatic system (Q2385362) (← links)
- Seven competing ways to recover the Michaelis-Menten equation reveal the alternative approaches to steady state modeling (Q2443867) (← links)
- The ``memory'' effect in a chain of biochemical reactions with a positive feedback is enhanced by substrate saturation described by Michaelis-Menten kinetics (Q2633582) (← links)
- Analysis of the Michaelis-Menten mechanism in an immobilised enzyme reactor (Q3365656) (← links)
- THE SINGLE ROOTS SIGMOID MODEL IN ENZYME KINETICS (Q3754468) (← links)
- (Q5156423) (← links)
