Abstract
The solubility and specific ATPase activity of carp myofibrils suspended in 5 and 50mM phosphate buffer (pH 6.8) were compared at three different storage temperatures, -4, -11, and -26°C, in the absence of neutral salts throughout a period of 167 days. Allocated ATPase activities in salt-soluble and salt-insoluble fractions were also calculated from solubility and specific ATPase activity. The extent of the decrease in solubility and in the four kinds of allocated ATPase activity in the salt-soluble fraction was smaller with a decrease in storage temperature at both buffer concentrations. It is suggested that myofibril insolubilization occurred without complete inactivation of ATPase activity.
