Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase

F. Orosz, Tania Y. Christova, J. Ovádi

Research output: Contribution to journalArticle

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Abstract

The effect of aldolase on the concentration-dependent kinetic behaviour of phosphofructokinase was investigated by means of covalently attached fluorescent probe and by using a kinetic approach. The dimeric form of kinase in equilibrium with the active tetramer interacts with the native aldolase with an apparent dissociation constant of 2.5 μM. Within this heterologous enzyme complex the phosphofructokinase is catalytically active probably because the aldolase binding to nascent kinase dimers might protect them against inactivation.

Original languageEnglish
Pages (from-to)1121-1128
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume147
Issue number3
DOIs
Publication statusPublished - Sep 30 1987

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Phosphofructokinases
Fructose-Bisphosphate Aldolase
Muscle
Muscles
Phosphotransferases
Kinetics
Fluorescent Dyes
Dimers
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase. / Orosz, F.; Christova, Tania Y.; Ovádi, J.

In: Biochemical and Biophysical Research Communications, Vol. 147, No. 3, 30.09.1987, p. 1121-1128.

Research output: Contribution to journalArticle

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