Summary
1. The activities of the two kinetic components (high and low affinity) of the microsomal 0-deethylation of 7-ethoxycoumarin have been measured in liver from patients with alcoholic cirrhosis and in normals. 2. The activity (expressed as pmol 7-OH coumarin formed/mg microsomal protein/min) of both components of the enzyme was significantly lower in alcoholic cirrhosis (high affinity=3.27±1.18, low affinity 60.9±11.6) than in normals (high affinity 9.43±2.37, low affinity 111.3±9.2). 3. These results are further evidence that there is a broad impairment of hepatic microsomal mono-oxygenase activity in alcoholic cirrhosis.
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Woodhouse, K.W., Williams, F.M., Mutch, E. et al. The effect of alcoholic cirrhosis on the two kinetic components (high and low affinity) of the microsomal 0-deethylation of 7-ethoxycoumarin in human liver. Eur J Clin Pharmacol 26, 61–64 (1984). https://doi.org/10.1007/BF00546710
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DOI: https://doi.org/10.1007/BF00546710