Purification and some properties of sn-glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae
| Autor: | Susan A. Sajer, Martin Straume, Joseph R. Merkel, Robert L. Hopfer |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
chemistry.chemical_classification
Ions Chromatography biology Saccharomyces cerevisiae Biophysics Dehydrogenase Glycerolphosphate Dehydrogenase Cell Biology Phosphate biology.organism_classification NAD Biochemistry Chromatography Affinity chemistry.chemical_compound Enzyme Glycerol-3-phosphate dehydrogenase chemistry Oxidoreductase Specific activity NAD+ kinase Molecular Biology |
| Zdroj: | Analytical biochemistry. 122(1) |
| ISSN: | 0003-2697 |
| Popis: | An NAD-dependent glycerol-3-phosphate dehydrogenase ( sn -glycerol-3-phosphate: NAD + oxidoreductase, EC 1.1.1.8) has been isolated and purified from Saccharomyces cerevisiae by affinity and exclusion chromatography. The enzyme was purified 5100-fold to a specific activity of 158. It has a molecular weight of approximately 31,000, a pH optimum between 6.8 and 7.2, and is sensitive to high-ionic-strength salt solutions. The enzyme is most strongly inhibited by phosphate and chloride ions. |
| Databáze: | OpenAIRE |
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