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PMID: 6087797 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Biochemical journal ·Vol. 220 ·No. 3 ·1984-06-15 ·Pages 825-33

Butterwith SC, Hopewell R, Brindley DN

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.

MeSH Terms
Animals Cations, Divalent/pharmacology Chromatography, Gel Chromatography, Ion Exchange Cyclohexanones/pharmacology Diacetyl/pharmacology Female Liver/enzymology Male Phosphatidate Phosphatase/antagonists & inhibitors,isolation & purification Phospholipids/pharmacology Phosphoric Monoester Hydrolases/isolation & purification Rats Sulfhydryl Reagents/pharmacology
Chemicals
Cations, Divalent Cyclohexanones Phospholipids Sulfhydryl Reagents 1,2-cyclohexanedione Phosphoric Monoester Hydrolases Phosphatidate Phosphatase Diacetyl
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Butterwith S C
Hopewell R
Brindley D N
References (30)
30 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2200825
Published
1984-06-15
Pages
825-33
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1153702
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2200825 PMC Full Text View journal details
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