Abstract
Carp myosin B was treated at 10°C in a medium containing 2.0M NaCl and 40mM Tris-maleate (pH 7.0) and its physico-chemical properties were examined with a lapse of time. During the treatment of myosin B with NaCl, (1) the viscosity (lnηr/C) of myosin B decreased, (2) the 22S component in the ultracentrifugal sedimentation pattern disappeared accompanied by a pro-duct of 5S component, (3) actomyosin fraction at void volume in the Sepharose C1-4B gel filtra-tion decreased with a formation of myosin fraction (elution volume/void volume=2.3), (4) of the supernatant from myosin B by salting out with 40% (NH4)2SO4 saturation, the intensities of bands corresponding to myosin (identified by SDS polyacrylamide gel electrophoretic pattern) increased, and (5) the amount of myosin bands increased further by the co-presence of ATP and NaCl.
These results suggested that the reaction between myosin B and a high concentration of NaCl may proceed through the dissociation process of myosin B into actin and myosin.
