Abstract
Carp myosin extracted with GUBA-STRAUB solution was purified by ultracentrifugation at 50, 000rpm in the presence of ATP and MgCl2 followed by precipitation at low ionic strength. The sedimentation coefficient, 6.4 S, and the intrinsic viscosity, 2.3dl/g, of the carp myosin were close to those of rabbit myosin. In amino acid composition, the carp myosin was very similar to rabbit myosin. While, on SDS-disc electrophoretic analysis, the rabbit myosin is reported to give a single band, of molecular weight 180-200×103, for the heavy chain as well as 3 bands, 25, 18 and 16×103, for the light cabins, the carp myosin presented a different pattern consisting of a 180-200 ×103 heavy chain band and only a single band, 17.5×103, of light chain.
By sedimentation analysis of the tryptic digests of the carp myosin, the carp myosin was found to be much more readily digestable than rabbit myosin. The carp LMM isolated from the digestion mixture was similar to rabbit LMM in sedimentation coefficient, 3 S, as well as in intrinsic viscosity, 1.3dl/g.
