Abstract
Tryptic (LMM Fr 1) and CNBr-treated (LMM-C) rod portion of myosin molecule were prepared from rabbit skeletal muscle myosin. An attempt was made to clarify the difference between LMM Fr 1 and LMM-C as measured by solubility and some physico-chemical techniques. The rigid structure of LMM Fr 1 melted into a random coil as temperature of the solution increased and the value of b0 and reduced viscosity did not show full recovery upon gradual cooling. The situation of LMM-C, on the other hand, showed the higher thermostability than LMM Fr 1. As stated in our previous paper,1) we have considered that the rod portion of myosin molecules is substantially thermostable.