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The first pharmacokinetic model described in the scientific literature [2] was in fact a PBPK model. It led, however, to computations intractable at that time. The focus shifted then to simpler models, [3] for which analytical solutions could be obtained (such solutions were sums of exponential terms, which led to further simplifications.)
The kinetic derivation applies to gas-phase adsorption. However, it has been mistakenly applied to solutions. The multiple-adsorbate case is covered in the competitive adsorption sub-section. The model assumes adsorption and desorption as being elementary processes, where the rate of adsorption r ad and the rate of desorption r d are given by
The models used in non-linear pharmacokinetics are largely based on Michaelis–Menten kinetics. A reaction's factors of non-linearity include the following: Multiphasic absorption: Drugs injected intravenously are removed from the plasma through two primary mechanisms: (1) Distribution to body tissues and (2) metabolism + excretion of the ...
The absorption rate of ethanol is typically modeled as a first-order kinetic process depending on the concentration gradient and specific membrane. The rate of absorption is fastest in the duodenum and jejunum, owing to the larger absorption surface area provided by the villi and microvilli of the small intestines.
[A] can provide intuitive insight about the order of each of the reagents. If plots of v / [A] vs. [B] overlay for multiple experiments with different-excess, the data are consistent with a first-order dependence on [A]. The same could be said for a plot of v / [B] vs. [A]; overlay is consistent with a first-order dependence on [B].
The absorption rate constant K a is a value used in pharmacokinetics to describe the rate at which a drug enters into the system. It is expressed in units of time −1. [1] The K a is related to the absorption half-life (t 1/2a) per the following equation: K a = ln(2) / t 1/2a. [1] K a values can typically only be found in research articles. [2]
The result is equivalent to the Michaelis–Menten kinetics of reactions catalyzed at a site on an enzyme. The rate equation is complex, and the reaction order is not clear. In experimental work, usually two extreme cases are looked for in order to prove the mechanism. In them, the rate-determining step can be: Limiting step: adsorption/desorption
Although the net formula for decomposition or isomerization appears to be unimolecular and suggests first-order kinetics in the reactant, the Lindemann mechanism shows that the unimolecular reaction step is preceded by a bimolecular activation step so that the kinetics may actually be second-order in certain cases. [7]