Abstract
Heating temperatures of 30-40°C and KCl concentrations of 0.1-0.5 M altered the denaturation mode of carp myofibrils. In 0.1 M KCl medium, heating temperature affected the denaturation of rod more significantly than of subfragment-1 (S-1), and a slow decrease in solubility at 30°C was accompanied by a slow denaturation of rod. KCl concentration at heating altered the denaturation mode differently at 30°C and 40°C. Increased KCl concentrations for heating reduced the rod denaturation rate at 40°C, but it was increased at 30°C. At concentrations above 0.3 M KCl, the denaturation rate for rod became identical to that for S-1 at both temperatures. Upon heating of chymotryptic digest of myofibrils, S-1 denaturation was similarly detected as in intact myofibrils, whereas practically no rod denaturation was detected. Thus, it was concluded that myosin structure connecting S-1 and rod has an important role in the denaturation process.
