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. 1984 Jun 15;220(3):825–833. doi: 10.1042/bj2200825

Partial purification and characterization of the soluble phosphatidate phosphohydrolase of rat liver.

S C Butterwith, R Hopewell, D N Brindley
PMCID: PMC1153702  PMID: 6087797

Abstract

A method is described by which the Mg2+-stimulated phosphatidate phosphohydrolase can be purified from the soluble fraction of liver from ethanol-treated rats. The increase in specific activity was about 416-fold. This involved purification by adsorption on calcium phosphate, chromatography on DE-52 DEAE-cellulose, separation on Ultrogel AcA-34 and chromatography on CM-Sepharose 6B. The effects of phosphatidylcholine, phosphatidate and Mg2+, Mn2+ and Zn2+ on the activity are described. Inhibitor studies indicate that the phosphohydrolase contains functional thiol groups and arginine residues.

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Selected References

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