Purification of ctp: cholinephosphate cytidylyl-transferase from pea stems |
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| Authors: | Molly J. Price-Jones John L. Harwood |
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| Affiliation: | Department of Biochemistry, University College, P.O. Box 78, Cardiff, CF1 1XL, U.K. |
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| Abstract: | ![]()
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 α2-macroglobulin and gel filtration. The purified enzyme had Km 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 Mg2+ and an Mr of 56000. It could not utilize phosphorylethanolamine and its activity was not stimulated by added phospholipids. |
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| Keywords: | Leguminosae pea stems cytidylyltransferase purification phosphatidylcholine metabolism. |
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