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

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

Resultado de la investigación: Article

1 Cita (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)4181-4184
Número de páginas4
PublicaciónBiochemistry
Volumen13
N.º20
DOI
EstadoPublished - 1 sep 1974

Huella dactilar

aminobutyraldehyde dehydrogenase
Pseudomonas
Purification
Oxidoreductases
Enzymes
Electrophoresis
Immune Sera
Succinate-Semialdehyde Dehydrogenase
Molecular Weight
Molecular weight
Sodium Dodecyl Sulfate
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Gels
Kinetics
3-aminopropionaldehyde
Substrates
Proteins

ASJC Scopus subject areas

  • Biochemistry

Citar esto

Callewaert, Denis M. ; Tchen, T. T. ; Rosemblatt, Mario S. / Purification and properties of 3-aminopropanal dehydrogenase from a pseudomonas species. En: Biochemistry. 1974 ; Vol. 13, N.º 20. pp. 4181-4184.
@article{7ecbe1d3bc4b4442ba5fcae753823cfc,
title = "Purification and properties of 3-aminopropanal dehydrogenase from a pseudomonas species",
abstract = "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.",
author = "Callewaert, {Denis M.} and Tchen, {T. T.} and Rosemblatt, {Mario S.}",
year = "1974",
month = "9",
day = "1",
doi = "10.1021/bi00717a018",
language = "English",
volume = "13",
pages = "4181--4184",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "20",

}

Purification and properties of 3-aminopropanal dehydrogenase from a pseudomonas species. / Callewaert, Denis M.; Tchen, T. T.; Rosemblatt, Mario S.

En: Biochemistry, Vol. 13, N.º 20, 01.09.1974, p. 4181-4184.

Resultado de la investigación: Article

TY - JOUR

T1 - Purification and properties of 3-aminopropanal dehydrogenase from a pseudomonas species

AU - Callewaert, Denis M.

AU - Tchen, T. T.

AU - Rosemblatt, Mario S.

PY - 1974/9/1

Y1 - 1974/9/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0016288566&partnerID=8YFLogxK

U2 - 10.1021/bi00717a018

DO - 10.1021/bi00717a018

M3 - Article

VL - 13

SP - 4181

EP - 4184

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 20

ER -