Purification of ctp: cholinephosphate cytidylyl-transferase from pea stems
| Autor: | Molly J. Price-Jones, John L. Harwood |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
chemistry.chemical_classification
Chromatography Size-exclusion chromatography Ion chromatography Cytidylyltransferase food and beverages Plant Science General Medicine Horticulture Biology biology.organism_classification Biochemistry Pisum Macroglobulin chemistry.chemical_compound Phosphorylethanolamine Enzyme chemistry Ammonium Molecular Biology |
| Zdroj: | Phytochemistry. 24:2523-2527 |
| ISSN: | 0031-9422 |
| DOI: | 10.1016/s0031-9422(00)80660-3 |
| Popis: | CTP:cholinephosphate cytidylyltransferase (EC 2.7.7.15) was purified from pea ( Pisum sativum ) stems. The purification involved ammonium sulphate fractionation, ion exchange chromatography, removal of proteases with α 2 -macroglobulin and gel filtration. The purified enzyme had K m values for phosphorylcholine and CTP of 2.1 mM and 0.55 mM respectively. It was found to have a pH optimum of 7.5, a requirement for Mg 2+ and an M r of 56000. It could not utilize phosphorylethanolamine and its activity was not stimulated by added phospholipids. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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