The effect of uremia on ethanol metabolism was investigated. Uremia was induced in male Sprague-Dawley rats by removal of approximately 85 per cent of the renal mass. Control animals had a sham operation. The mean activity of alcohol dehydrogenase was markedly increased in the uremic rats to 2.12 ± 0.13 (S.E.M.) μmoles per milligram of protein per hour as compared with a control value of 1.39 ± 0.13 μmoles per milligram of protein per hour (p < 0.001). There were no changes in the activity of the microsomal ethanol oxidizing system, in catalase activity present in the microsomes, or in the rates of ethanol disappearance from the blood. Uremia resulted in decreases in microsomal cytochrome P-450, but no changes in cytochrome b5, NADPH-cytochrome c reductase, or in the activities of aniline hydroxylase and aminopyrine demethylase. The increase in alcohol dehydrogenase activity could not be reproduced by incubation of liver from a normal rat with uremic rat plasma, uremic human serum, or urea. Also, the increase in the enzyme activity was not associated with changes in leucocyte ascorbic acid levels. The cause and physiologic significance of the increase in alcohol dehydrogenase activity in uremia remain to be elucidated.
|Original language||English (US)|
|Number of pages||7|
|Journal||The Journal of laboratory and clinical medicine|
|State||Published - Dec 1975|
ASJC Scopus subject areas
- Pathology and Forensic Medicine