Archives of Microbiology

, Volume 120, Issue 3, pp 255–262

Electron microscopic study on the quaternary structure of the isolated particulate alcohol-acetaldehyde dehydrogenase complex and on its identity with the polygonal bodies of Clostridium kluyveri

  • R. Lurz
  • F. Mayer
  • G. Gottschalk
Article

DOI: 10.1007/BF00423073

Cite this article as:
Lurz, R., Mayer, F. & Gottschalk, G. Arch. Microbiol. (1979) 120: 255. doi:10.1007/BF00423073

Abstract

The alcohol-acetaldehyde dehydrogenase complex of Clostridium kluyveri has been separated from contaminating β-hydroxybutyryl-CoA dehydrogenase by repeated precipitation with manganese and ammonium sulfate. Mn++ was required for maximum alcohol dehydrogenase activity.

The molecular weight of the enzyme complex was 194,000 as determined by sucrose density gradient centrifugation. The enzyme complex has been shown to contain two types of subunits with molecular weights of 55,000±2,600 and 42,000±1,200, respectively which are arranged in “H”-shaped particles.

In solutions with an ionic strength above 25 mM the enzyme complex precipitated in the form of lumps as has been shown with specific ferritin-conjugated antibodies. These lumps are assumed to be aggregated polygonal bodies present in C. kluyveri.

Key words

Alcohol dehydrogenase Acetaldehyde dehydrogenase Clostridium kluyveri Electron microscopy Polygonal bodies Enzyme complex 

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • R. Lurz
    • 1
  • F. Mayer
    • 1
  • G. Gottschalk
    • 1
  1. 1.Institut für Mikrobiologie der UniversitätGöttingenFederal Republic of Germany
  2. 2.Max-Planck-Institut für Molekulare GenetikBerlin-Dahlem