Abstract
When akazara striated adductor myosin was heat-treated at various pHs, inactivation of Ca-ATPase activity proceeded more slowly at pH 7.0 to 8.0 than in higher or lower pH range. Then, heat-inactivation rates of akazara myosin were determined in 0.6M KCl at pH 7.0, using Ca-ATPase, Mg-ATPase, actin-activated Mg-ATPase and superprecipitation activities as parameters.
The results obtained showed that superprecipitation activity was most susceptible, and that the latter three activities decreased in two steps consisting of a fast and a slow change.
