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.
Research Article| June 01 1974
Interaction of aldolase with the troponin–tropomyosin complex of bovine muscle
F. M. Clarke;
C. J. Masters;
Biochem J (1974) 139 (3): 785-788.
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
F. M. Clarke, C. J. Masters, D. J. Winzor; Interaction of aldolase with the troponin–tropomyosin complex of bovine muscle. Biochem J 1 June 1974; 139 (3): 785–788. doi: https://doi.org/10.1042/bj1390785
Download citation file: