Rat adipose tissue phosphatidic acid phosphatase: lack of effect of nucleotides on cytosolic enzyme activity.

A. al-Shurbaji, Lars Berglund

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The soluble phosphatidic acid phosphatase from rat adipose tissue was partially purified using ammonium sulfate fractionation and hydroxyapatite chromatography. Administration of ethanol has been found to increase phosphatidic acid phosphatase activity. The enzyme activity has been found to be dependent on magnesium ions with maximal activity at 2-5 mM magnesium. The enzyme displays an apparent pH optimum of 7.0. The activity of the enzyme is not affected by addition of ATP or ADP, in contrast with the results for hepatic phosphatidic acid phosphatase. The results suggest that these two enzymes may be regulated by different mechanisms and that they may thus represent two different types of isoenzyme.

Original languageEnglish (US)
Pages (from-to)680-683
Number of pages4
JournalActa chemica Scandinavica (Copenhagen, Denmark : 1989)
Volume43
Issue number7
StatePublished - Aug 1989
Externally publishedYes

ASJC Scopus subject areas

  • Chemical Engineering(all)

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