Purification and properties of 3-aminopropanal dehydrogenase from a pseudomonas species

Denis M. Callewaert, T. T. Tchen, Mario S. Rosemblatt

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1 Citation (Scopus)


3-Aminopropanal dehydrogenase has been purified from a Pseudomonas species. The enzyme has high activity toward 3-aminopropanal and low inherent activity toward 4-aminobutanal and succinic semialdehyde as substrate. The enzyme has a molecular weight of 213,000-226,000 as determined by gel filtration and polyacrylamide gel electrophoresis with reference proteins. Electrophoresis in sodium dodecyl sulfate gave a subunit molecular weight of 74,000 indicating that this is a three subunit enzyme. Purified 3-aminopropanal dehydrogenase does not cross-react with antisera to succinic semialdehyde dehydrogenase but does cross-react with antisera to 4- aminobutanal dehydrogenase. While 3-aminopropanal dehydrogenase and 4-aminobutanal dehydrogenase are similar in size and antigenicity, their induction patterns and kinetic constants differ significantly. It is suggested that there is a close evolutionary relationship between these two enzymes.

Original languageEnglish
Pages (from-to)4181-4184
Number of pages4
Issue number20
Publication statusPublished - 1 Sep 1974

ASJC Scopus subject areas

  • Biochemistry


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