Purification and properties of 4 aminobutanal dehydrogenase from a Pseudomonas species

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

Resultado de la investigación: Article

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

Huella dactilar

aminobutyraldehyde dehydrogenase
Pseudomonas
Purification
Electrophoresis
Enzymes
Molecular Weight
Molecular weight
Substrates
Sodium Dodecyl Sulfate
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Gels
Kinetics
Proteins

ASJC Scopus subject areas

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

Citar esto

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Purification and properties of 4 aminobutanal dehydrogenase from a Pseudomonas species. / Callewaert, D. M.; Rosemblatt, M. S.; Tchen, T. T.

En: Journal of Biological Chemistry, Vol. 249, N.º 6, 1974, p. 1737-1741.

Resultado de la investigación: Article

TY - JOUR

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AU - Rosemblatt, M. S.

AU - Tchen, T. T.

PY - 1974

Y1 - 1974

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AB - 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.

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