Add time:08/14/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes the assay method, purification procedure, and properties of phosphorylcholine -cytidyl transferase. The activity of the enzyme can be studied either by measuring the amount of cytidine diphosphate choline (CDP-choline) synthesized from CTP and labeled phosphorylcholine, or by following the pyrophosphorolytic cleavage of synthetic labeled CDP-choline. In either case, the absorption of CDP-cocholine on charcoal under conditions in which phosphorylcholine is not absorbed is the essential step. As it is somewhat more convenient to follow the pyrophosphorolysis, this procedure is described in the chapter. The enzyme is highly specific for cytosine-containing cofactors and for phosphorylcholine; however, deoxycytidine diphosphate choline and deoxycytidine triphosphate are also active. The reaction catalyzed by phosphorylcholine-cytidyl transferase is readily reversible, but the equilibrium constant has not been accurately measured. The enzyme requires divalent cations for optimum activity. At low concentrations, manganese and magnesium ions are equally effective, but at higher concentrations manganese appears to be inhibitory.

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