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Abstract
Phosphorylcholine cytidyltransferase, the enzyme which catalyzes the transfer of phosphorylcholine to cytidine 5'-triphosphate to form CDP-choline, was studied for the first time in human neonatal lung. The assay of product synthesis was linear for 10-20 min and up to 12 mg protein. The pH optimum was 6-6.5. The Km of CTP was 2.0 times 10- minus 3 M, and the Km of phosphorylcholine was 0.25 times 10- minus 3 M. The true Vmax was 10 nmol CDP-choline/mg protein/10 min. The enzyme was stable under frozen conditions. Oxygen had no apparent affect on enzyme activity.
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