Key result
Calcium and magnesium activate crab myofibril ATPase activity while KCl decreases it, mirroring rabbit actomyosin.
The actomyosin system of a crab is essentially similar to that of a rabbit regarding KCl concentration dependence on ATPase activity.
No immediate clinical cardiology relevance; extends rabbit data confirming conserved actomyosin ATPase regulation across species.
KCl concentration dependence on the ATPase activity of myofibrils and of myosin B was studied using crab muscle. 1 ) Without addition of bivalent cations, the ATPase activities of these actomyosin systems were vrey low. 2 ) By addition of 100 μM Ca++ or 2 mM Mg++ these ATPase activities were activated.3) These activated ATPases were decreased with increasing the KCl concentration. From these results, it was indicated that the actomyosin system of a crab is essentially similar to that of a rabbit.
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Masaki et al. (1970) studied this question. Potassium chloride (KCl) was evaluated on ATPase activity of myofibrils and myosin B. The ATPase activity of crab myofibrils and myosin B was activated by calcium or magnesium and decreased with increasing KCl concentrations, demonstrating similarity to rabbit actomyosin systems.
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