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.
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. 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). These results are further evidence that there is a broad impairment of hepatic microsomal mono-oxygenase activity in alcoholic cirrhosis.
D015660:7-Alkoxycoumarin O-Dealkylase; D000428:Alcohol Drinking; D005260:Female; D006801:Humans; D007700:Kinetics; D008104:Liver Cirrhosis, Alcoholic / Q000378:metabolism*; D008111:Liver Function Tests; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D008875:Middle Aged; D010105:Oxygenases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D012907:Smoking
D011506:Proteins; D010105:Oxygenases; D015660:7-Alkoxycoumarin O-Dealkylase