Cephalopod alcohol dehydrogenase: purification and enzymatic characterization

M. Rosario Fernández, Hans Jörnvall, Alberto Moreno, Rudolf Kaiser, Xavier Parés

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22 Citations (Scopus)


Octopus, squid and cuttle-fish organs were examined for alcohol dehydrogenase activity. Only one form was detectable, with properties typical of mammalian class III alcohol dehydrogenase. The corresponding protein was purified from octopus and enzymatically characterized. Ionexchange and affinity chromatography produced a pure protein in excellent yield (73%) after 1600-fold purification. Enzymatic parameters with several substrates were similar to those for the human class III alcohol dehydrogenase, demonstrating a largely conserved function of the enzyme through wide lines of divergence covering vertebrates, cephalopods and bacteria. The results establish the universal occurrence of class III alcohol dehydrogenase and its strictly conserved functional properties in separate living forms. The absence of other alcohol dehydrogenases in cephalopods is compatible with the emergence of the ethanol-active class I type at a later stage, in lineages leading to vertebrates. © 1993.
Original languageEnglish
Pages (from-to)235-238
JournalFEBS lett.
Issue number3
Publication statusPublished - 16 Aug 1993


  • Alcohol dehydrogenase
  • Cephalopod enzyme
  • Enzymatic properties
  • Glutathione-dependent formaldehyde dehydrogenase
  • Octopus protein
  • Protein evolution


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