The heat-induced gelation of myosin was optimally developed at temperatures between 60° and 70°C and at pH 6.0 as studied quantitatively by measuring shear modulus of myosin in 0.6M KCl. No difference was observed in the gelation profile, when KCl was replaced by NaCl. The shear modulus of the gel formed at 65°C and pH 6.0 increased proportionally to the 1.8 power of myosin concentration. Although the heat gelling ability of myosin as measured by the shear modulus did not increase with increasing salt concentration from 0.4–1.0M, irrespective of storage time at 0°C of the stock myosin solution (0.6M KCl) or suspension (0.1M KCl), it varied drastically with time of storage at salt concentrations between 0.1 and 0.3. This variation in shear modulus at O.1–0.3M KCl was apparent due to the storage conditions. These changes in the salt concentration dependence of the heat gelation of myosin corresponded well with the changes in solubility of myosin during storage. Studies on selected physico-chemical properties of the original stock myosin during storage indicated gradual increase in viscosity with little inactivation of ATPase as well as very slight decrease in sulfhydryl content, suggesting the spontaneous transformation (aggregation) of myosin molecules to a less soluble state.