Interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate

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Population

Acto-heavy meromyosin (HMM) and acto-subfragment 1 (S-1) solutions

Comparison

Presence of adenosine triphosphate under… vs Absence of ATP and presence of ATP at 0.1 M KCl

Design

Preclinical

Authors

Discussion

Suggests predominant refractory myosin states at peak activation; leaves open their role in regulating cardiac contractility.

Population

Acto-heavy meromyosin (HMM) and acto-subfragment 1 (S-1) solutions

Intervention

Presence of adenosine triphosphate (ATP) under conditions where actin-activated ATPase is close to its maximal value

Comparator

Absence of ATP (completely complexed) and presence of ATP at 0.1 M KCl (almost completely dissociated)

Outcome

Viscosity, turbidity, and laser-light fluctuation autocorrelationssurrogate

Under conditions of maximal actin activation, most heavy meromyosin and subfragment 1 occur in a refractory state unable to bind to actin.

Fraser et al. (1975) studied this question.

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