The isolation and characterization of the tropomyosin binding component (TN-T) of bovine cardiac troponin

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Abstract
The tropomyosin binding component (TN-T) of troponin was purified from bovine cardiac muscle using a combination of ion exchange chromatographies in the presence of urea. Sedimentation equilibrium experiments suggest a molecular weight for cardiac TN-T of 36,300 .+-. 2000, consistent with a value of 37,000 .+-. 1000 determined by polyacrylamide gel electrophoresis. Calculations based upon circular dichroism spectra indicate an apparent .alpha.-helical content of 43 .+-. 3% for TN-T. Polyacrylamide gel electrophoresis and the effects of the Ca binding component (TN-C) upon the solubility of TN-T suggest that the 2 cardiac troponin components can interact with each other. Cosedimentation analysis of solutions containing cardiac tropomyosin and TN-T provide evidence for complex formation involving these 2 proteins. The data presented on the physical and chemical properties of TN-T, as well as the interaction studies indicate that the cardiac muscle regulatory system operates in a manner similar to that proposed for skeletal muscle.

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