PMID: 6110708Mar 1, 1981Paper

Properties of a CDP-diglyceride hydrolase from guinea pig brain

Journal of Neurochemistry
H G RittenhouseB W Agranoff

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.

References

Mar 25, 1975·Biochimica Et Biophysica Acta·R H Michell
Jan 1, 1979·Journal of Neurochemistry·J N Hawthorne, M R Pickard
Jul 15, 1976·Biochemical Pharmacology·C H DonnellyD L Murphy
Jan 1, 1976·Analytical Biochemistry·A Bensadoun, D Weinstein
Dec 3, 1971·Biochimica Et Biophysica Acta·C W Cotman, D A Matthews
Dec 1, 1972·Archives of Neurology·S G EliassonR R Fox
Oct 1, 1972·Analytical Biochemistry·P J Geiger, S P Bessman
Jul 1, 1961·Biochemical Pharmacology·G L ELLMANR M FEATHER-STONE

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Citations

Sep 14, 1982·Biochimica Et Biophysica Acta·P P Murthy, B W Agranoff
Jan 1, 1985·Progress in Lipid Research·P S Sastry

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