Purification and properties of 4 aminobutanal dehydrogenase from a Pseudomonas species

D. M. Callewaert, M. S. Rosemblatt, T. T. Tchen

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20 Citations (Scopus)


4 Aminobutanal dehydrogenase has been purified from a Pseudomonas species. The enzyme has high activity toward aminoaldehydes (4 aminobutanal or 3 aminopropanal) and low activity toward succinic semialdehyde as substrate. The kinetic constants, effect of p hyroxymercuribenzoate, and pH profile with different substrates are documented. The enzyme has a molecular weight of 228,000 as determined by gel filtration and polyacrylamide gel electrophoresis with reference proteins. Electrophoresis in sodium dodecyl sulfate gave a subunit molecular weight of 75,000 indicating that this is a three subunit enzyme.

Original languageEnglish
Pages (from-to)1737-1741
Number of pages5
JournalJournal of Biological Chemistry
Issue number6
Publication statusPublished - 1974

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)
  • Molecular Biology
  • Cell Biology


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