Abstract
Summary
An increase in the assay temperature of hepatic alcohol dehydrogenase (ADH) activity, from 25 to 50-60°, with ethanol as the substrate, led to a stimulation of enzyme activity. The stimulation of the hepatic ADH (not observed with yeast ADH) was reversible if the heated samples were allowed to cool to room temperature and then assayed at 25°. Only at the elevated temperature (50-60°) could ADH activity be detected in normal rat or human plasma. The increased sensitivity resulting from thermal activation of ADH may prove useful for studying the enzyme in crude preparations, measuring ADH activity with substrates normally providing low activity (e.g., 17-β-hydroxy-5-β-androston-3-one), or measuring serum ADH activity in patients with various types of liver injury.
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