We will create a one-compartment model for alcohol breakdown in the human body. We just look at the change of the blood alcohol concentration after the alcohol is fully absorbed into the body (or is administered in a clinical trial through an IV bolus injection). So we look for a suitable initial value problem
for certain initial concentration
at time
. What we should write in place of the dots is determined by the rate of elimination of alcohol by enzymes in the liver.
A reasonable assumption is that an enzyme is more busy with the elimination of alcohol the more it is likely to interact with an alcohol molecule, and that the frequency of interaction is larger when the alcohol concentration is greater in the tissues where the enzyme is. When there is a rapid exchange between the bloodstream and the liver, then we may suppose that the concentration in the tissues is equal or proportional to the blood alcohol concentration. So
for some positive parameter
. The solution is
Unfortunately, this model does not describe properly measured blood alcohol levels after alcohol consumption: At a high alcohol permillage the elimination seems to reach a maximum speed.
When alcohol enters the liver it is converted to acetaldehyde by the enzyme alcohol dehydrogenase (ADH) and cytochrome P450 (CYP2E1). Acetaldehyde is toxic and carcinogenic, but it is converted to acetate by the enzyme aldehyde dehydrogenase (ALDH). The first reaction is reversible, the second is not.
What goes wrong in the first attempt at modelling of alcohol breakdown? Essentially, the point is that we have not considered yet in the model that the interaction between the enzyme and the alcohol molecule takes time to reach proper conditions to form an enzyme-alcohol complex.
We assume that the average waiting time to realize an interaction between the enzyme and the alcohol molecule is inversely proportional to the blood alcohol concentration: , say
for some positive parameter
. Once the enzyme molecule and the alcohol molecule "found each other" there is still an average processing time
needed. We assume that this processing time does not depend on the concentration
but is constant. The average time required for the enzyme molecule to convert one alcohol molecule is set equal to the sum of the waiting and processing time. For conversion of
alcohol molecules we expect the time
needed for one enzyme molecule to achieve this equals
Then we get the following expression for the reaction rate
per enzyme molecule, that is, the number of alcohol molecules converted per unit of time:
Substitution of the assumed expression for the average waiting time then gives
But in the liver is more than one enzyme molecule present and therefore we must for the conversion rate of alcohol through the liver multiply the previous formula by a constant
and then we have:
where
is the volume of distribution of alcohol in the central compartment. We rewrite this model as
where
is called the
Michaelis-Menten constant (value is about 30 mg/L), and
is the
maximum elimination rate of alcohol (equivalent to approximately 200 mg/min).
For high blood alcohol concentration can be neglected in comparison with and we get that . This means that alcohol elimination at high alcohol concentrations takes place linearly over time: about the alcohol amount of 1 glass of alcoholic beverage (a standard unit) will be eliminated as per hour.
For low blood alcohol concentration can be neglected in comparison with and we get that . This means that alcohol elimination is described in case of low alcohol concentrations by an exponential decay model.
Wagner, JG Patel, JA (1972). Variations in the absorption and elimination rates, or ethyl alcohol in a single subject. Res Commun Chem Pathol Pharmacol 4, 61-76.