Key result
Increasing KCl concentration steadily decreases the Vmax of actin-activated myosin ATPase activity while F-actin sliding velocity remains unchanged, suggesting ATPase activity is not linked to motility.
In vitro studies of skeletal muscle myosin suggest that ATPase activity is not necessarily tightly coupled to motility.
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Challenges assumed ATPase-motility coupling in skeletal myosin; leaves open cardiac isoform relevance.
Takiguchi et al. (1990) studied this question. KCl concentration was evaluated on actin-activated myosin ATPase activity, myosin binding to actin, and the velocity of myosin-induced actin sliding. Increasing KCl concentration steadily decreases the Vmax of actin-activated myosin ATPase activity while F-actin sliding velocity remains unchanged, suggesting ATPase activity is not linked to motility.
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