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 Citations (Scopus)

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

Fingerprint

Phosphatidate Phosphatase
Phosphatases
Enzyme activity
Nucleotides
Rats
Enzymes
Tissue
Magnesium
Acids
Isoenzymes
Administrative data processing
Adenosinetriphosphate
Ammonium Sulfate
Durapatite
Fractionation
Chromatography
Hydroxyapatite
Adenosine Diphosphate
Ethanol
Adenosine Triphosphate

ASJC Scopus subject areas

  • Chemical Engineering(all)

Cite this

@article{308a3157a7814e7083313fb42b1a9e45,
title = "Rat adipose tissue phosphatidic acid phosphatase: lack of effect of nucleotides on cytosolic enzyme activity.",
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.",
author = "A. al-Shurbaji and Lars Berglund",
year = "1989",
month = "8",
language = "English (US)",
volume = "43",
pages = "680--683",
journal = "Acta Chemica Scandinavica",
issn = "0904-213X",
publisher = "Royal Society of Chemistry",
number = "7",

}

TY - JOUR

T1 - Rat adipose tissue phosphatidic acid phosphatase

T2 - lack of effect of nucleotides on cytosolic enzyme activity.

AU - al-Shurbaji, A.

AU - Berglund, Lars

PY - 1989/8

Y1 - 1989/8

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0024716805&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024716805&partnerID=8YFLogxK

M3 - Article

C2 - 2486133

AN - SCOPUS:0024716805

VL - 43

SP - 680

EP - 683

JO - Acta Chemica Scandinavica

JF - Acta Chemica Scandinavica

SN - 0904-213X

IS - 7

ER -