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Cephalopod alcohol dehydrogenase: purification and enzymatic characterization
Author(s) -
Fernández M.Rosario,
Jörnvall Hans,
Moreno Alberto,
Kaiser Rudolf,
Parés Xavier
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80934-m
Subject(s) - alcohol dehydrogenase , cephalopod , enzyme , biochemistry , biology , alcohol , dehydrogenase , affinity chromatography , ethanol , fishery
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.