Abstract
Thermal inactivation of Ca2+ ATPase of squid myofibrils was significantly suppressed in the presence of Ca2+. Monomeric myosin content decreased much faster than Ca2+ ATPase inactivation in Ca medium, which was well explained by fast rod denaturation. In contrast, rod denaturation was slower than S-1 in EDTA medium. The decrease in monomeric myosin content was explained by faster S-1 denaturation. Comparing the S-1 and rod denaturation rates at a fixed temperature, it was concluded that S-1 denaturation was suppressed by Ca2+ whereas the rod denaturation was not. An unfolding experiment with isolated myosin rod confirmed that there was no stabilizing effect of Ca2+ on myosin rod. It was concluded that significant stabilization of the S-1 portion by Ca2+ generated the apparently different myosin denaturation patterns in the two media.
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