Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties
| Autor: | Wen Ni Chang, Tzu Fun Fu, Hung Chang Lin |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Male
animal structures Leucovorin Dehydrogenase medicine.disease_cause Isozyme Chromatography Affinity Pichia Cell Line In vivo Escherichia coli medicine Animals Humans Cloning Molecular Protein Structure Quaternary Zebrafish chemistry.chemical_classification Aldehydes Oxidoreductases Acting on CH-NH Group Donors biology fungi biology.organism_classification Recombinant Proteins Yeast Protein Structure Tertiary Isoenzymes Enzyme Biochemistry chemistry Chromatography Gel Electrophoresis Polyacrylamide Gel Female Function (biology) Biotechnology |
| Zdroj: | Protein Expression and Purification. 72:217-222 |
| ISSN: | 1046-5928 |
| DOI: | 10.1016/j.pep.2010.04.003 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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