Aspects on the phosphorylation of muscle phosphofructokinase by protein kinase C--inhibition by phosphofructokinase stabilisers |
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| Authors: | F A Nettelblad P O Forsberg E Humble L Engstr?m |
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| Affiliation: | 1. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, PR China;2. Precision Livestock and Nutrition Unit, Gembloux Agro-Bio Tech, University of Liège, Passage de Déportés 2, Gembloux, Belgium;1. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China;2. Precision Livestock and Nutrition Unit, Gembloux Agro-Bio Tech, University of Liège, Passage de Déportés 2, Gembloux, Belgium;3. Department of Food Science, Faculty of Science, University of Copenhagen, DK-1958 Frederiksberg, Denmark |
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| Abstract: | Our report presents data on the phosphorylation of muscle phosphofructokinase by Ca2+-activated, phospholipid-dependent protein kinase. We have found a stoichiometrical phosphorylation (about 1.5 mol per mol subunit), and a low apparent Km (about 0.7 microM). These data speak in favor of a physiological role for the reaction, as does the fact that phosphofructokinase from a new species (rat) was successfully phosphorylated. On the other hand we present the hitherto unpublished circumstance that the phosphorylation is inhibited by conditions that stabilise the activity of phosphofructokinase. This fact makes us question the true significance of this reaction. |
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