| Abstract: | The preparation of subfragment HMM-S-1 of Rabbit skeletal myosin was achieved by a proteolytic digestion of myofibrils in the presence of EDTA. The product was purified on DEAE-cellulose and its characteristics were compared to those of HMM-S-1 prepared by other methods. In denaturing conditions the HMM-S-1 was shown to be fragmented into a small number of well defined polypeptides. The molecular weights of which were: 68000, 52000, 26000, 235000, 21000 and 14000 daltons. A certain degree of heterogeneity was revealed by the elution profile as well as the quantitative study of polyacrylamide gel electrophoresis. |
