Abstract
Calmodulin (CaM) was purified from squid mantle muscle using hydrophobic chromatography. Relative molecular mass of the purified CaM deduced form the SDS-PAGE was exactly the same as that of bovine brain. Comparison of bovine brain and squid CaM indicates that each activates phosphodiesterase identically and that their activation curves are superimposable. Distribution of CaM in the squid tissues was also examined by measuring the activation level of PDE activity. The content of squid CaM in generative organ and fin is relatively higher than in pancreas, liver, and mantle muscle.
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