Key result
Ultracentrifugal studies demonstrated a labile interaction between aldolase and the troponin-tropomyosin complex from bovine muscle that is suppressed by fructose 1,6-diphosphate.
The study demonstrates an interaction between aldolase and the troponin-tropomyosin complex in bovine muscle, suggesting alternative binding sites to F-actin for aldolase on skeletal muscle thin filaments.
Supports metabolic modulation of thin filaments in animal muscle; leaves open any relevance to human contractile regulation.
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.
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Clarke et al. (1974) studied this question. Aldolase and troponin-tropomyosin complex interaction was evaluated on Interaction between aldolase and the troponin-tropomyosin complex. Ultracentrifugal studies demonstrated a labile interaction between aldolase and the troponin-tropomyosin complex from bovine muscle that is suppressed by fructose 1,6-diphosphate.
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