Key result
In the presence of ATP, N-ethylmaleimide modified heavy meromyosin and actin are almost completely dissociated, existing mostly in a refractory state unable to bind to actin.
Population
In vitro biochemical model studying N-ethylmaleimide modified heavy meromyosin and actin
Comparison
Presence of adenosine triphosphate and varying… vs Absence of adenosine triphosphate (ATP)
Design
Preclinical
Authors
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No immediate clinical implications; leaves open the rate-limiting role of myosin transitions in actin regulation.
In the presence of ATP, N-ethylmaleimide modified heavy meromyosin exists mostly in a refractory state unable to bind actin, suggesting the transition to a nonrefractory state is the rate-limiting step during actin activation.
Mulhern et al. (1975) studied this question. N-ethylmaleimide modified heavy meromyosin vs. Normal heavy meromyosin was evaluated on Binding to actin during ATP hydrolysis. In the presence of ATP, N-ethylmaleimide modified heavy meromyosin and actin are almost completely dissociated, existing mostly in a refractory state unable to bind to actin.
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