In a 1936 paper by Neymark and Widmark¹ it was shown that the rate of oxidation of alcohol in the body is a constant. To avoid the delays encountered by diffusion, the alcohol was introduced by intravenous injection into the bodies of test animals and it was observed that the decrease in the blood followed a straight line descent. This is what one would expect if an enzyme was involved in the breakdown of the alcohol molecule. Since the alcohol has to combine with the catalyst, a limited amount of catalyst limits the rate of reaction. As the amount of alcohol in the blood increases above a critical limit the reaction rate tends to level off. This value is very small so the rate of decrease appears constant for typical concentrations of alcohol. It can be shown that the reaction rate is proportional to the product of the concentration of catalyst and the value of ρ in the formula below.
A group of enzymes, alcohol dehydrogenase, is required to metabolize alcohol.
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¹ Neymark, M. and Widmark, E. M. P. (1936), Zur Frage der Kinetik des Aethylalkoholumsatzes im Organismus. Skandinavisches Archiv Für Physiologie, 73: 283–290. doi: 10.1111/j.1748-1716.1936.tb01471.x
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