Interaction of aldolase with the troponin-tropomyosin complex of bovine muscle.
Ultracentrifugal studies of mixtures of aldolase and the troponin-tropomyosin complex from bovine muscle showed the existence of a labile interaction between these two myofibrillar constituents in imidazole buffers, pH6.8, I 0.02-0.10 (mol/l), and the suppression of the reaction by fructose 1,6-diphosphate. Analysis of the sedimentation-velocity patterns suggests the binding of more than 2 molecules of troponin-tropomyosin/molecule of aldolase. The results illustrate the necessity of considering additional or alternative sites to F-actin to account for the observed binding of aldolase to the thin filaments of skeletal muscle.
D000199:Actins; D002021:Buffers; D002499:Centrifugation, Density Gradient; D003956:Dialysis; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D007093:Imidazoles; D007700:Kinetics; D009124:Muscle Proteins / Q000378:metabolism*; D011485:Protein Binding; D014335:Tropomyosin / Q000378:metabolism*; D014461:Ultracentrifugation
D000199:Actins; D002021:Buffers; D007093:Imidazoles; D009124:Muscle Proteins; D014335:Tropomyosin; D005634:Fructose-Bisphosphate Aldolase