D. Callewaert, M. Rosemblatt, T. Tchen
Mar 25, 1974
Citations
1
Influential Citations
18
Citations
Journal
The Journal of biological chemistry
Abstract
Abstract 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-hydroxymercuribenzoate, 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.