Abstract
Myosins from various vertebrate species were heat-denatured. The resulting aggregates were dissolved by boiling with 8 M urea-0.5% 2-mercaptoethanol and dialyzed against water. The dialyzate turned to a transparent gel. The gel melted on heating, but set to gel again on cooling. The gel was reproduced on rehydrating the once dehydrated gel. Heat-denaturation of the starting myosin did not affect the elasticity of the product. The solubilized gel showed the same electrophoretic pattern as that of intact myosin and showed two bands that were due to a myosin heavy chain and light chain in the elution pattern. The reduced viscosity of the solubilized gel increased, as the myosin concentration in the dialyzate increased.
