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 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 language | English |
|---|---|
| Pages (from-to) | 1737-1741 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 249 |
| Issue number | 6 |
| State | Published - 1974 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology