Abstract
Carp myosin B(2-3mg/ml) was treated at 10°C with 2.OM NaCl or KCl in the presence of various concentrations of sorbitol. During the treatment of myosin B, changes in ATP sensitivity, the amount of denatured actin, and thermal inactivation mode of Ca-ATPase were investigated with a lapse of time. The ATP sensitivity irreversibly decreased and denatured actin increased with the duration of salt treatment. Thermal inactivation mode of Ca-ATPase changed from a single first order step to a biphasic first order process by the salt treatment. The changes induced by NaCl were relatively larger than those by KCl, and sorbitol reduced these changes. After the treatment with 2.0M NaCl for 3h, dissociation of myosin from myosin B was recognized by ultracentrifugal sedimentation analysis and gel filtration profile on Sepharose-CL-4B followed by SDS-polyacrylamide gel electrophoretic analysis, and such salt-induced production of myosin monomer was also reduced by the treatment in the presence of sorbitol. These results showed that sorbitol suppressed the dissociation of myosin B into actin and myosin induced by high concentration of salt.
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