[65d] Phosphorylcholine-glyceride transferase

Add time:08/15/2019    Source:sciencedirect.com

Publisher SummaryThis chapter describes the assay method, purification procedure, and properties of phosphorylcholine-glyceride transferase. The most convenient method for the measurement of this enzyme is to determine the amount of radioactive lecithin formed from synthetic cytidine diphosphate choline (CDP-choline) labeled with choline-l,2-C14 in the presence of D-a,fl-diglyceride. At the end of the experiment the lecithin is extracted with ethanol, taken up in chloroform, and washed repeatedly with aqueous salt solutions to remove all traces of the unreacted, water-soluble CDP-choline. An aliquot of the chloroform solution is then plated in an aluminum cup and counted. Phosphorylcholine-glyceride transferase is widely distributed in animal tissue and is also found in plants and yeast. A convenient source of the enzyme is commercially available fresh-frozen chicken liver, from which a particulate fraction consisting largely of microsomal material is prepared. The enzyme is highly specific for CDP-choline but is active with the closely related deoxycytidine diphosphate choline. It is also quite specific for α,β -diglycerides of the D configuration. The reaction catalyzed by the phosphoryleholineglyeeride transferase is readily reversible; thus the monophosphate diester linkage in lecithin must be regarded as an energy-rich bond.

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