The spreading of monolayers of myosin

The spreading of the muscle proteins myosin and actomyosin depends both on the salt solution in which the proteins are dissolved and on the solution on which they are spread. The spreading is more complete the lower the concentration of the salt solution in which the proteins are dissolved and the higher the salt concentration of the solutions on which the proteins are spread. This effect seems to be due partially to the difference in density allowing the spread droplets a longer life on the surface, and partially to the effect of salt on the charge of the protein. A change in the pH of the substrate has a smaller effect than a change in the salt concentration. Heavy metals like Cu⁺⁺ or Zn⁺⁺, inhibit spreading almost completely. The dependence of spreading on these salts and on time was investigated in detail.The effect of the different salts was also compared with the effect of different phosphate compounds. It was noted that the above substances, including the different salts, phosphate compounds, and heavy metals, affect the mechanism of spreading but not films already spread. The viscosity of these fibrillar proteins was compared with other proteins in the monomolecular film state and in myosin an unusually high viscosity was found.