Studies on the Stability of Soluble and Immobilized Alcohol Dehydrogenase from Yeast Mitochondria

  • M. J. Brougham
  • D. B. Johnson


Alcohol dehydrogenases have been the subject of detailed investigations both by pure and applied scientists. Much information is now available on the primary structures of horse liver and of yeast alcohol dehydrogenases and detailed X-ray crystallographic data have been provided for both enzymes (1). On the other hand horse liver enzyme has been considered as a potential tool in organic syntheses (2), and the yeast enzyme has been used in studies on coenzyme regeneration and recycling (3). Among the barriers to the exploitation of these enzymes are their high costs and the failure, to date, to provide immobilized preparations of suitable stability. One possible approach to solving this problem is to select an enzyme stable in the soluble form, and then to find conditions of immobilization and of operation optimal for enzyme stability.


Alcohol Dehydrogenase Mitochondrial Enzyme Soluble Enzyme Cytosol Enzyme Yeast Mitochondrion 
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Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • M. J. Brougham
    • 1
  • D. B. Johnson
    • 1
  1. 1.Biochemistry DepartmentUniversity CollegeGalwayIreland

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