Differences in thermal stability of frog and rabbit alpha alpha- and alpha beta-tropomyosins determined by optical rotatory dispersion.
Frog and rabbit alpha alpha- and alpha beta-tropomyosins were purified, and their thermal stabilities determined by use of optical rotatory dispersion. The tropomyosins were found to be virtually completely helical at 5 degrees C. Regions of different thermal stabilities were seen for all tropomyosins. Rabbit and frog alpha alpha-tropomyosin show very similar thermal properties, with main transitions near 47-49 degrees C. The main transition for frog alpha beta-tropomyosin is at 32 degrees C. The results show that the alpha beta-tropomyosins are less stable than the alpha alpha-forms. Only thermal transitions of the alpha beta-forms appear to be correlated with the body temperatures of the animals.
D000818:Animals; D004355:Drug Stability; D046911:Macromolecular Substances; D009905:Optical Rotatory Dispersion / Q000379:methods; D011487:Protein Conformation; D011817:Rabbits; D011896:Rana temporaria; D013816:Thermodynamics; D014335:Tropomyosin
D046911:Macromolecular Substances; D014335:Tropomyosin