Influence of Ethanol Oxidation Rate on the Lactate/Pyruvate Ratio and Phosphorylation State of the Liver in Fed Rats.

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Abstract
The effect of the ethanol oxidation rate on the interaction between the phosphorylation state (the [ATP]/[ADP] .times. [HPO4]2- ratio) and the redox state (the free [NAD+]/[NADH] ratio) of the liver cytosol was studied in intact fed rats. The rate of ethanol oxidation was inhibited to different degrees with pyrazole. The ethanol oxidation rate had no influence on the liver lactate level but correlated significantly with the pyruvate level. A significant correlation was found between the ethanol oxidation rate and the lactate/pyruvate ratio. The rate of ethanol oxidation correlated significantly with the liver 3-phosphoglycerate level. No change in the glyceraldehyde-3-phosphate level was found. No correlation was found between the ethanol oxidation rate and the glyceraldehyde-3-phosphate/3-phosphoglycerate redox couple. Ethanol administration slightly increased the liver ATP level, but the simultaneous administration of pyrazole eliminated this effect. Other adenine nucleotides and HPO42- were not changed. The changes in the rate of ethanol oxidation had no effect on the phosphorylation state in the fed liver. In the fed liver the phosphorylation state was so well stabilized that the redox level had no influence.