Purification and properties of 4 aminobutanal dehydrogenase from a Pseudomonas species

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

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

20 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)1737-1741
Número de páginas5
PublicaciónJournal of Biological Chemistry
Volumen249
N.º6
EstadoPublicada - 1974

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Medicina (todo)
  • Biología molecular
  • Biología celular

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