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Co-Metabolism of Menadione (Vitamin K3) and the Ethanol in Human Liver Fractions

NCJ Number
224759
Journal
Problems of Forensic Sciences Volume: 73 Dated: 2008 Pages: 21-29
Author(s)
Krzysztof Tutaj; Grzegorz Buszewicz; Grzegorz Teresinski; Roman Madro
Date Published
2008
Length
9 pages
Annotation
Results are presented from an experiment conducted on whether the addition of menadione (vitamin K3) to human liver homogenates leads to accelerated oxidation of ethanol (Et-OH) and if so, whether mitochondria and the microsomal ethanol-oxidizing system (MEOS) are involved, and whether the acceleration depends on the activity of quinine reductase (QR).
Abstract
Results include: (1) acceleration of ethanol (Et-OH) oxidation by menadione occurs in human liver homogenates and (2) comparison of area under the curve (AUC) values shows that in vitro quinone reductase, mitochondrial NADH: ubiquinone oxidoreductase and MEOS are involved in the vitamin K-accelerated rate of Et-OH oxidation. The findings demonstrate that mitochondria, MEOS and also QR activity are involved in the menadione, increased rate of Et-OH oxidation. The conversion of ethanol into acetaldehyde, catalyzed by alcohol dehydrogenase (ADH) with simultaneous reduction of NAD+ to NADH, is found to be a rate-limiting step in the ethanol metabolism pathway. In this study concerning the possibilities of increasing ethanol metabolism, a system was used which contained subcellular fractions of human liver homogenates, an ethanol concentration and menadone in equimolar amount to Et-OH. Figures, table, and references

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