Wheat gluten-based diet retarded ethanol metabolism by altering alcohol dehydrogenase and not carnitine status in adult rats.

The purpose of these experiments was to examine the factors which regulate ethanol metabolism in vivo. Since the major pathway for ethanol removal requires flux through hepatic alcohol dehydrogenase, the activity of this enzyme was measured and found to be 2.9 μmol/(min∙g liver). Ethanol disappearance was linear for over 120 min in vivo and the blood ethanol fell 0.1 mM/min; this is equivalent to removing 20 μmol ethanol/min and would require that flux through alcohol dehydrogenase be about 60% of its measured maximum velocity. To test whether ethanol metabolism was limited by the rate of removal of one of the end products (NADH) of alcohol dehydrogenase, fluoropyruvate was infused to reoxidize hepatic NADH and to prevent NADH generation via flux through pyruvate dehydrogenase. There was no change in the rate of ethanol clearance when fluoropyruvate was metabolized. Furthermore, enhancing endogenous hepatic NADH oxidation by increasing the rate of urea synthesis (converting ammonium bicarbonate to urea) did not augment the steady-state rate of ethanol oxidation. Hence, transport of cytoplasmic reducing power from NADH into the mitochondria was not rate limiting for ethanol oxidation. In contrast, ethanol oxidation at the earliest time periods could be augmented by increasing hepatic urea synthesis.

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Ethanol metabolism in subiects possessing typical and atypical liver alcohol dehydrogenase

Clinical Pharmacology & Therapeutics ◽

10.1002/cpt196786824 ◽

1967 ◽

Vol 8 (6) ◽

pp. 824-829 ◽

Cited By ~ 65

Author(s):

John A. Edwards ◽

David A. Price Evans

Keyword(s):

Alcohol Dehydrogenase ◽

Ethanol Metabolism ◽

Liver Alcohol Dehydrogenase

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Functional Assessment of Human Alcohol Dehydrogenase Family in Ethanol Metabolism: Significance of First-Pass Metabolism

Alcoholism Clinical and Experimental Research ◽

10.1111/j.1530-0277.2006.00139.x ◽

2006 ◽

Vol 30 (7) ◽

pp. 1132-1142 ◽

Cited By ~ 80

Author(s):

Shou-Lun Lee ◽

Gar-Yang Chau ◽

Chung-Tay Yao ◽

Chew-Wun Wu ◽

Shih-Jiun Yin

Keyword(s):

Alcohol Dehydrogenase ◽

Functional Assessment ◽

Ethanol Metabolism ◽

First Pass Metabolism ◽

First Pass ◽

Pass Metabolism

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Ethanol metabolism by the rat heart and alcohol dehydrogenase activity

Canadian Journal of Biochemistry ◽

10.1139/o76-079 ◽

1976 ◽

Vol 54 (6) ◽

pp. 539-545 ◽

Cited By ~ 14

Author(s):

G. W. Forsyth ◽

H. T. Nagasawa ◽

C. S. Alexander

Keyword(s):

Alcohol Dehydrogenase ◽

Dehydrogenase Activity ◽

Rat Heart ◽

Specific Activity ◽

Ph Dependence ◽

Ethanol Metabolism ◽

Minor Role ◽

Alcohol Dehydrogenase Activity ◽

A Minor

Rat hearts perfused with oxygenated buffer containing [1-14C]ethanol metabolized small amounts of the ethanol to carbon dioxide. Very sensitive techniques are required to separate the resulting 14CO2 from the ethanol. This metabolism is not inhibited by levels of pyrazole which markedly inhibit NAD dependent liver alcohol dehydrogenase (EC 1.1.1.1). In vitro studies suggest that NADP functions as a cofactor for the rat heart alcohol dehydrogenase activity of crude heart homogenates. The kinetic parameters, the specific activity, and the pH dependence of the enzyme activity measured in these experiments suggest that it may have a minor role in ethanol metabolism by the rat.

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