Michaelis-Menton equation kinetics

Michaelis-Menton equation/kinetics This equation, which is central to enzymology, describes the relationship between the initial rate of reaction (v) and the substrate concentration (Q. It gives the initial rate of reaction as v = V ax C/(K +C) where V ax is the maximum velocity of reaction, C is the concentration of substrate and is the Michaelis-Menton constant. C is equal to the Michaelis-Menton constant when vis 50% of micro- A prefix meaning small. 

Non-linear pharmacokinetics are much less common than linear kinetics. They occur when drug concentrations are sufficiently high to saturate the ability of the liver enzymes to metabolise the drug. This occurs with ethanol, therapeutic concentrations of phenytoin and salicylates, or when high doses of barbiturates are used for cerebral protection. The kinetics of conventional doses of thiopentone are linear. With non-linear pharmacokinetics, the amount of drug eliminated per unit time is constant rather than a constant fraction of the amount in the body, as is the case for the linear situation. Non-linear kinetics are also referred to as zero order or saturation kinetics. The rate of drug decline is governed by the Michaelis-Menton equation ... 

Equation 9 is a hyperbolic relationship, similar to the Michaelis-Menton equation derived for enzyme kinetics (104) the Langmuir equation as applied to adsorption on soils (105), and an adaptation of these models for dechlorination by Fe that we published previously (13). As such, all four models are capable of describing site saturation phenomena commonly found in heterogenous systems however, only the new model (equations 8 and 9) explicitly distinguishes thermodynamically-related parameters from the kinetic constants. 

The potential for such systems to respond radically to small changes in the concentration of effector molecules arises because their kinetic behavior can be described by the Michaelis-Menton equation (see). At steady state, the fraction of protein P in active form (P /P, ,) depends on the rate constants of the ac-... 

This equation is known as the Michaelis-Menton equation. A plot of rate r versus substrate concentration [S] (Figure 2.20) shows that the rate equation follows first-order kinetics fp = (k/kuAS] at low substrate concentrations and zero-order kinetics r = k ed. high substrate concentrations. The tangent to versus [S] plot drawn at [S] = 0 intersects r = k at a point corresponding to [S] = k - This method of tangent can be used to determine the kinetic parameters k and k - Alternatively, we can write the rate equation in linear form as (l/fp) = kM/k) l/[S]) + (1/k) by inverting Equation 2.169. Thus, by making a linear plot of... 

Verify if the given data confirm to the Michaelis-Menton kinetic rate equation... 

Estimation of Kinetic parameters of Enzyme Catalysed Reaction S % Michaelis - Menton rate equation % Reaction rate - (-ra) = (kl Cs)/(Km+Cs)... 

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