January 1, 1982Proceedings of the National Academy of SciencesOpen Access

Inhibition of actomyosin ATPase by vanadate.

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Population

Actin-myosin subfragment-1 (SF-1) or actin-heavy meromyosin (in vitro biochemical model)

Comparison

ADP and vanadate (Vi) vs ADP alone or normal ATPase cycle

Design

Preclinical

Authors

CGCharles C. GoodnoUniversity of Iowa ETEdwin W. TaylorOldham Council

Discussion

Member takes

Implication

Vanadate-ADP inhibition of myosin ATPase should not change cardiac practice; leaves open refinement of cross-bridge kinetics in animal models.

Structured PICO

Population

Actin-myosin subfragment-1 (SF-1) or actin-heavy meromyosin (in vitro biochemical model)

Intervention

ADP and vanadate (Vi)

Comparator

ADP alone or normal ATPase cycle

Outcome

ATPase activity and dissociation of ligandssurrogate

Vanadate and ADP form a stable complex with myosin that inhibits actomyosin ATPase activity, acting as a stable analogue of the myosin-ADP-phosphate complex generated in the normal ATPase cycle.

Cite This Study

Goodno et al. (1982) studied this question.

synapsesocial.com/papers/6a20a8389ca8a48788f36f3f https://doi.org/10.1073/pnas.79.1.21

View Full Paper

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Implication

Vanadate-ADP inhibition of myosin ATPase should not change cardiac practice; leaves open refinement of cross-bridge kinetics in animal models.

Inhibition of actomyosin ATPase by vanadate.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Inhibition of actomyosin ATPase by vanadate.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider