10-formyltetrahydrofolate has been researched along with propionaldehyde* in 1 studies
1 other study(ies) available for 10-formyltetrahydrofolate and propionaldehyde
| Article | Year |
|---|---|
Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties.
10-Formyltetrahydrofolate dehydrogenase from zebrafish has been cloned and expressed in both Escherichia coli and yeast. In addition, the N-terminal and C-terminal domains have also been cloned and expressed. Each expressed protein was purified to homogeneity and structural and kinetic properties determined. These studies show that the zebrafish enzyme is structurally and catalytically very similar to the enzymes from mammalian sources, suggesting that zebrafish can be used to study the in vivo function of 10-formyltetrahydrofolate dehydrogenase. Topics: Aldehydes; Animals; Cell Line; Chromatography, Affinity; Chromatography, Gel; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Female; Humans; Isoenzymes; Leucovorin; Male; Oxidoreductases Acting on CH-NH Group Donors; Pichia; Protein Structure, Quaternary; Protein Structure, Tertiary; Recombinant Proteins; Zebrafish | 2010 |