Properties of a CDP‐Diglyceride Hydrolase from Guinea Pig Brain

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Abstract
Enzymatic hydrolysis of the pyrophosphate bond of CDP‐diglyceride (CDP‐DG), previously shown to occur in bacteria, is demonstrable in mammalian tissues. Activity was enriched in a lysosomal fraction obtained from guinea pig cerebral cortex and was purified 92‐fold relative to the homogenate by a combination of XM‐300 ultrafiltration and DEAE‐cellulose column chromatography. When incubated with CDP‐dipalmitin, the purified enzyme produced stoichiometric amounts of CMP and phosphatidate. dCDP‐DG served as a substrate, while ADP‐DG was an inhibitor, as were 5′‐AMP and 5′‐dAMP. CDP‐DG hydrolysis was not affected by the presence of excess amounts of CDP‐choline, CDP‐glycerol, sodium pyrophosphate, or cyclic 3′,5′‐AMP.