Purification and properties of 3-aminopropanal dehydrogenase from a Pseudomonas species.
نویسندگان
چکیده
4-Aminobutanal dehydrogenase has been purified from a Pseudomonas species. The enzyme has high activity toward aminoaldehydes (4-aminobutanal or d-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.
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عنوان ژورنال:
- Biochemistry
دوره 13 20 شماره
صفحات -
تاریخ انتشار 1974