Skip to content
Research Article Open access CC BY 4.0

Purification of Alcohol Dehydrogenase Enzyme from Chicken Liver and Immobilization Onto Florisil

Havva Ersoz, Nuri Gulesci, Ramazan Bilgin

Asian Journal of Research in Biochemistry · pp. 6–14 · Published 20 Aug 2022

10.9734/ajrb/2022/v10i430230

Abstract

The enzyme alcohol dehydrogenase (ADH) is a dimeric enzyme in which each of its subunits has a Zn2+ metal-containing catalytic domain and a cofactor binding domain. This enzyme converts alcohol into an aldehyde. In this article, the activity of the enzyme was investigated by applying the immobilization process directly to the alcohol dehydrogenase enzyme purified and activated florisil from the chicken liver. For this purpose, homogenization of chicken liver was achieved and its supernatants were separated by applying the ultracentrifugation process to the resulting homogenate. Then, % ammonium precipitation, dialysis, and ion exchange chromatography processes were performed, respectively. As a result of these processes, the hepatic alcohol dehydrogenase was purified 150.3 times compared to the coarse homogenate, and the specific activity of the enzyme was determined to be 0.631 U/mg protein. The activity of the enzyme directly immobilized was found to be 0.034 U/mg protein.

Alcohol dehydrogenase florisil liver ion exchange chromatography

References (12)

  1. 1 PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT [DOI]
  2. 2 Carrier-bound Immobilized Enzymes: Principles, Application and Design
  3. 3 The genetics of alcohol dependence and alcohol-related liver disease [DOI]
  4. 4 ZINC, A COMPONENT OF YEAST ALCOHOL DEHYDROGENASE [DOI]
  5. 5 Immobilization and kinetics of catalase onto magnesium silicate [DOI]
  6. 6 Adipose tissue autophagy and homeostasis in alcohol-induced liver injury [DOI]
  7. 7 Alcohol Dehydrogenase from Sheep Liver: Purification, Characterization and Impacts of Some Antibiotics [DOI]
  8. 8 Content of acetylcholine receptor and antibodies bound to receptor in myasthenia gravis, experimental autoimmune myasthenia gravis, and Eaton‐Lambert syndrome [DOI]
  9. 9 Ethanol induced cardiovascular disease [DOI]
  10. 10 Purification of copper-zinc-superoxide dismutase and catalase from human erythrocytes by copper-chelate affinity chromatography [DOI]
  11. 11 Investigation of liver alcohol dehydrogenase catalysis using an NADH biomimetic and comparison with a synthetic zinc model complex [DOI]
  12. 12 The purification and properties of an alcohol dehydrogenase from mouse liver [DOI]

Cited by 4

Showing 2 of 4 known citations — external sources report more than can currently be individually listed.

Article metrics

Real usage data collected on this platform.

64

Page views

0

PDF downloads

23

Outbound clicks

4

Citations

Views over time

Views by country

Approximate, from request IP at view time — not citizenship or institution. Countries with fewer than 5 views are grouped as "Other".

Traffic sources

Referring site, by host.

Views and downloads exclude known bots/crawlers. Citations combines this platform's own DOI-resolved index with each external source's own reported total — see Cited by above for individually listed citing works. Last refreshed 0 seconds ago.