Ethanol elimination in regenerating rat liver: the roles of alcohol dehydrogenase and acetaldehyde.
The rate of ethanol elimination in vivo was studied with rats in which the energy consumption of the liver was increased by partial hepatectomy. Immediately after partial hepatectomy the activity of alcohol dehydrogenase in the liver remnant was not changed from that of the livers of sham-operated controls, but the rate of ethanol removal was significantly faster. Twenty-four h after the partial hepatectomy the activity of alcohol dehydrogenase was only 48 % of the activity measured in unoperated control rats. Therefore it is concluded that in normal liver the activity of ADH is in excess. In partially hepatectomized rats the rate of ethanol elimination was linearly correlated with the activity of alcohol dehydrogenase, which suggests that when the rate of NADH reoxidation is markedly increased, as in regenerating rat liver, the rate of ethanol elimination may be limited by the activity of alcohol dehydrogenase. The activity of aldehyde dehydrogenase and the concentration of acetaldehyde in the tail blood were not significantly changed from the level of unoperated rats during oxidation of ethanol.
D000079:Acetaldehyde / Q000378:metabolism*; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D000431:Ethanol / Q000378:metabolism*; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D008115:Liver Regeneration; D008291:Malate Dehydrogenase / Q000378:metabolism; D008297:Male; D051381:Rats
D000431:Ethanol; D000429:Alcohol Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D008291:Malate Dehydrogenase; D000445:Aldehyde Oxidoreductases; D001219:Aspartate Aminotransferases; D000079:Acetaldehyde