Pages that link to "Item:Q751534"

The following pages link to Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios (Q751534):

Displaying 23 items.

• A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model (Q398592) (← links)
• A note on the kinetics of suicide substrates (Q454298) (← links)
• Solution method for the transformed time-dependent Michaelis-Menten enzymatic reaction model (Q500690) (← links)
• Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution (Q551897) (← links)
• Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. II: Time hierarchy, enzymatic rate laws, and erythrocyte metabolism (Q809004) (← links)
• The kinetic effect of the inactivation of the enzyme--substrate complex in an enzymatic reaction with slow-binding inhibition (Q814739) (← links)
• Enzyme kinetics at high enzyme concentration (Q886790) (← links)
• On the validity of the steady state assumption of enzyme kinetics (Q1108228) (← links)
• A kinetic analysis of coupled (or auxiliary) enzyme reactions (Q1633265) (← links)
• Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements (Q1797422) (← links)
• Mechanism equivalence in enzyme-substrate reactions: Distributed differential delay in enzyme kinetics (Q1878862) (← links)
• New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase (Q1959308) (← links)
• Extreme properties of the initial rate of the four-stage reaction of enzyme catalyzed ATP hydrolysis (Q2046286) (← links)
• Interpretation of \(V/K\) isotope effects for enzymatic reactions exhibiting multiple isotopically sensitive steps (Q2202387) (← links)
• Kinetic behaviour of proenzymes activation in the presence of different inhibitors for both activating and activated enzymes (Q2209924) (← links)
• Reduced models of networks of coupled enzymatic reactions (Q2263461) (← links)
• Maini's many contributions to mathematical enzyme kinetics: a review (Q2328226) (← links)
• Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics (Q2328227) (← links)
• A transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stability (Q2441094) (← links)
• Why substrate depletion has apparent first-order kinetics in enzymatic digestion (Q2500381) (← links)
• Enzyme kinetics of multiple alternative substrates (Q5928777) (← links)
• An algebraic mathematical model for non-competitive enzyme inhibitors with slow and fast subsystems (Q6106839) (← links)
• Two different types of kinetics, where the initial rate increases faster or slower than the reactant concentration, can coexist on bell-shaped kinetic dependencies (Q6168216) (← links)