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Purification and comparative studies of alcohol dehydrogenases.

Authors
  • Tsai, C S
  • Al-Kassim, L S
  • Mitton, K P
  • Thompson, L E
  • Van Es, C
  • White, J H
Type
Published Article
Journal
Comparative biochemistry and physiology. B, Comparative biochemistry
Publication Date
Jan 01, 1987
Volume
87
Issue
1
Pages
79–85
Identifiers
PMID: 3301186
Source
Medline
License
Unknown

Abstract

Alcohol dehydrogenases from various animal and plant sources were purified by a common procedure which employed DEAE, Sephadex-G100 and affinity chromatographies. The procedure achieves an 80-130 fold purification for animal enzymes. However, only a 5-15 fold purification for plant enzymes was attained because of the instability of these enzymes. Purified alcohol dehydrogenases from animal and plant sources differ in coenzyme and substrate specificities. The enzymes from mammalian, avian and fish livers display aldehyde oxidizing and esterolytic activities in addition to alcohol oxidizing activity. However, the enzymes from plants and yeast show only the oxidative activity toward alcohols. Chemical modifications have been performed to identify amino acid residues which are essential to the oxidative and esterolytic activities of alcohol dehydrogenases.

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