Incubation of salted surimi paste at 25°C generated the 150 and 70 kDa fragments. Two additional bands (bands a and b) migrating between myosin heavy chain monomer (HC) and dimer (HC2) were detected as well. Western blotting analysis of the above bands with anticarp subfragment-1 (s-1) HC antibody and sequencing of the amino terminal region of the 70 kDa fragment identified these 150 and 70 kDa fragments as heavy meromyosin (HMM)- and light meromyosin (LMM)-like fragments, respectively. The bands a and b are suggested to be the cross-linked product of HC and the 150 kDa, and two 150 kDa fragments, respectively. Thus, two distinct events, degradation and cross-linking of myosin HC, could occur on the same myosin molecule. These products were proved to be all aggregates losing salt-solubility.