Interactions between beta-enolase and creatine kinase in the cytosol of skeletal muscle cells.
We studied interactions in vivo between the cytosolic muscle isoform of creatine kinase (M-CK) and the muscle isoform of 2-phospho-D-glycerate hydrolyase (beta-enolase) in muscle sarcoplasm by incubating glycerol-skinned fibres with FITC-labelled beta-enolase in the presence or absence of free CK. A small amount of bound beta-enolase was observed in the presence of large concentrations of CK. The mobility of enolase was measured in cultured satellite cells by modulated-fringe-pattern photobleaching. FITC-labelled beta-enolase was totally mobile in both the presence and the absence of CK but its diffusion coefficient was slightly lower in the presence of CK. This suggests a weak interaction in vivo between enolase and CK.
Foucault
G
G
Gènes et Protéines Musculaires, EP CNRS 1088, Centre scientifique d'Orsay, bâtiment 430, F 91405 Orsay cedex, France. georges.foucault@bpc.u-psud.fr
Vacher
M
M
Cribier
S
S
Arrio-Dupont
M
M
D000818:Animals; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D003402:Creatine Kinase / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology*; D004058:Diffusion; D016650:Fluorescein-5-isothiocyanate; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000378:metabolism; D008856:Microscopy, Fluorescence; D018485:Muscle Fibers, Skeletal / Q000166:cytology / Q000201:enzymology; D018482:Muscle, Skeletal / Q000166:cytology / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D010777:Photochemistry; D011485:Protein Binding; D011817:Rabbits
D007527:Isoenzymes; D003402:Creatine Kinase; D010751:Phosphopyruvate Hydratase; D016650:Fluorescein-5-isothiocyanate