Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase
Autor: | Tania Y. Christova, Judit Ovádi, Ferenc Orosz |
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Rok vydání: | 1987 |
Předmět: |
Enzyme complex
biology Chemistry Muscles Phosphofructokinase-1 Aldolase B Aldolase A Allosteric regulation Biophysics Fructose-bisphosphate aldolase Cell Biology In Vitro Techniques Biochemistry Dissociation (chemistry) Kinetics Spectrometry Fluorescence Allosteric Regulation Tetramer Fructose-Bisphosphate Aldolase biology.protein Animals Rabbits Molecular Biology Phosphofructokinase |
Zdroj: | Biochemical and Biophysical Research Communications. 147:1121-1128 |
ISSN: | 0006-291X |
DOI: | 10.1016/s0006-291x(87)80186-9 |
Popis: | 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 microM. Within this heterologous enzyme complex the phosphofructokinase is catalytically active probably because the aldolase binding to nascent kinase dimers might protect them against inactivation. |
Databáze: | OpenAIRE |
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