Skip to main content
NCBI home page
British Journal of Clinical Pharmacology logoLink to British Journal of Clinical Pharmacology
. 1976 Jun;3(3):461–467. doi: 10.1111/j.1365-2125.1976.tb00622.x

Ethanol oxidizing enzyme activites in liver disease.

J Dow, N Krasner, A Goldberg
PMCID: PMC2958761  PMID: 973973

Abstract

1 The activites of hepatic alcohol dehydrogenase, catalase and the reduced nicotinamide adenine dinucleotide phosphate (NADPH) dependent ethanol oxidizing system were determined in liver biopsies from nine patients with liver disease and seven control subjects with non evidence of liver disease. 2 Alcohol dehydrogenase and catalase activites were significantly lower in the patients with liver disease. 3 The activity of the NADPH dependent ethanol oxidizing system was significantly greater in the patients with liver disease, when its activity was expressed in terms of mg protein or g wet weight liver. 4 It is suggested that the greater activity of the NADPH dependent system may compensate for the low alcohol dehydrogenase activites found in patients with liver disease and maintain normal rates of ethanol metabolism.

Full text

PDF
461

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Carter E. A., Isselbacher K. J. Hepatic microsomal ethanol oxidation. Mechanism and physiologic significance. Lab Invest. 1972 Sep;27(3):283–286. [PubMed] [Google Scholar]
  2. Clark C. G., Senior J. R. Ethanol clearance and oxidation of ethanol to carbon dioxide in persons with and without liver disease. Gastroenterology. 1968 Dec;55(6):670–676. [PubMed] [Google Scholar]
  3. FIGUEROA R. B., KLOTZ A. P. Alterations of liver alcohol dehydrogenase and other hepatic enzymes in alcoholic cirrhosis. Gastroenterology. 1962 Jul;43:10–12. [PubMed] [Google Scholar]
  4. Goldberg L., Rydberg U. Inhibition of ethanol metabolism in vivo by administration of pyrazole. Biochem Pharmacol. 1969 Jul;18(7):1749–1762. doi: 10.1016/0006-2952(69)90164-6. [DOI] [PubMed] [Google Scholar]
  5. Goldstein D. B. A method for assay of catalase with the oxygen cathode. Anal Biochem. 1968 Sep;24(3):431–437. doi: 10.1016/0003-2697(68)90148-6. [DOI] [PubMed] [Google Scholar]
  6. Hochstein P., Utley H. Hydrogen peroxide detoxication by glutathione peroxidase and catalase in rat liver homogenates. Mol Pharmacol. 1968 Nov;4(6):574–579. [PubMed] [Google Scholar]
  7. Kater R. M., Carulli N., Iber F. L. Differences in the rate of ethanol metabolism in recently drinking alcoholic and nondrinking subjects. Am J Clin Nutr. 1969 Dec;22(12):1608–1617. doi: 10.1093/ajcn/22.12.1608. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. LUNDQUIST F., WOLTHERS H. The kinetics of alcohol elimination in man. Acta Pharmacol Toxicol (Copenh) 1958;14(3):265–289. doi: 10.1111/j.1600-0773.1958.tb01164.x. [DOI] [PubMed] [Google Scholar]
  10. Lieber C. S., DeCarli L. M. Ethanol oxidation by hepatic microsomes: adaptive increase after ethanol feeding. Science. 1968 Nov 22;162(3856):917–918. doi: 10.1126/science.162.3856.917. [DOI] [PubMed] [Google Scholar]
  11. Lieber C. S., DeCarli L. M. Reduced nicotinamide-adenine dinucleotide phosphate oxidase: activity enhanced by ethanol consumption. Science. 1970 Oct 2;170(3953):78–80. doi: 10.1126/science.170.3953.78. [DOI] [PubMed] [Google Scholar]
  12. Maier K. P., Volk B., Hoppe-Seyler G., Gerok W. Urea-cycle enzymes in normal liver and in patients with alcoholic hepatitis. Eur J Clin Invest. 1974 Jun;4(3):193–195. doi: 10.1111/j.1365-2362.1974.tb00391.x. [DOI] [PubMed] [Google Scholar]
  13. Mezey E., Robles E. A. Effects of phenobarbital administration on rates of ethanol clearance and on ethanol-oxidizing enzymes in man. Gastroenterology. 1974 Feb;66(2):248–253. [PubMed] [Google Scholar]
  14. Mezey E., Tobon F. Rates of ethanol clearance and activities of the ethanol-oxidizing enzymes in chronic alcoholic patients. Gastroenterology. 1971 Nov;61(5):707–715. [PubMed] [Google Scholar]
  15. RAEIHAE N. C., KOSKINEN M. S. EFFECT OF NON-IONIC SURFACE-ACTIVE SUBSTANCE ON THE ACTIVATION OF ALCOHOL DEHYDROGENASE OF RAT LIVER HOMOGENATES. Life Sci. 1964 Oct;3:1091–1095. doi: 10.1016/0024-3205(64)90123-7. [DOI] [PubMed] [Google Scholar]
  16. Schoene B., Fleischmann R. A., Remmer H., von Oldershausen H. F. Determination of drug metabolizing enzymes in needle biopsies of human liver. Eur J Clin Pharmacol. 1972 Mar;4(2):65–73. doi: 10.1007/BF00562499. [DOI] [PubMed] [Google Scholar]
  17. Videla L., Bernstein J., Israel Y. Metabolic alterations produced in the liver by chronic ethanol administration. Increased oxidative capacity. Biochem J. 1973 Jun;134(2):507–514. doi: 10.1042/bj1340507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. von Wartburg J. P., Papenberg J., Aebi H. An atypical human alcohol dehydrogenase. Can J Biochem. 1965 Jul;43(7):889–898. doi: 10.1139/o65-102. [DOI] [PubMed] [Google Scholar]

Articles from British Journal of Clinical Pharmacology are provided here courtesy of British Pharmacological Society

RESOURCES