Properties of serum alcohol dehydrogenase in Nigerians with primary hepatoma.

Abstract

The serum activity of alcohol dehydrogenase was determined in healthy controls and in patients with liver diseases. The mean activity in hepatoma (6.4 +/- 1.0U/L) was significantly higher (P less than 0.05) than the mean values in liver cirrhosis (2.7 +/- 0.5U/L); hepatitis (4.3 +/- 1.0U/L), obstructive jaundice (2.9 +/- 0.5U/L) and healthy controls (0.7 +/- 0.1U/L). Alcohol dehydrogenase purified by CM-cellulose chromatography from the sera of patients with hepatoma had a higher affinity for butanol long chain saturated and unsaturated alcohols than the purified enzyme from healthy controls. Similarly, hepatoma alcohol dehydrogenase oxidized ethanol very poorly (KM = 154 microM) when compared with that from healthy controls (KM = 40.2 microM). Hepatoma alcohol dehydrogenase was inhibited by pyrazole while those of other liver diseases and the healthy controls were not. These properties of serum alcohol dehydrogenase may prove useful in the early diagnosis of hepatoma since biochemical changes occur before morphological changes in the development of cancer.

• Authors: I O Ogunleye, S O Olusi
• Journal: Annals of clinical biochemistry (Ann Clin Biochem) Vol. 28 ( Pt 6) Pg. 606-12 (Nov 1991) ISSN: 0004-5632 [Print] England
• PMID: 1663717 (Publication Type: Journal Article)

Chemical References

• Alcohol Dehydrogenase

Topics

• Adult
• Aged
• Aged, 80 and over
• Alcohol Dehydrogenase (blood, isolation & purification)
• Carcinoma, Hepatocellular (diagnosis)
• Clinical Enzyme Tests
• Diagnosis, Differential
• Electrophoresis, Polyacrylamide Gel
• Enzyme Stability
• Female
• Humans
• Kinetics
• Liver Neoplasms (diagnosis)
• Male
• Middle Aged
• Molecular Weight
• Nigeria