February 20, 1990Biochemistry

Cryoenzymic studies on actomyosin ATPase. Evidence that the degree of saturation of actin with myosin subfragment 1 affects the kinetics of the binding of ATP

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Population

Actomyosin subfragment 1 (acto-S1) and actin

Comparison

Varying degrees of saturation of actin with… vs S1 alone and acto heavy meromyosin (acto-HMM)

Design

Preclinical

Authors

CTChiara TesiIstituto di Fisiologia Clinica FTFranck TraversInstitut de Recherche en Infectiologie de Montpellier TBThomas E. BarmanIndian Institute of Technology Bombay

Discussion

Member takes

Implication

Saturation modulates acto-S1 ATP kinetics; extends in vitro cross-bridge models but leaves open physiological relevance in cardiac muscle.

Structured PICO

Population

Actomyosin subfragment 1 (acto-S1) and actin

Intervention

Varying degrees of saturation of actin with myosin subfragment 1 (S1)

Comparator

S1 alone and acto heavy meromyosin (acto-HMM)

Outcome

Kinetics of ATP binding and dissociationsurrogate

The degree of saturation of actin with myosin subfragment 1 significantly affects the kinetics of ATP binding, with a sharp transition observed near saturation.

Limitations

Lack of structural information makes the abrupt dependence of ATP binding kinetics upon the S1 to actin ratio difficult to explain

Cite This Study

Tesi et al. (1990) studied this question.

synapsesocial.com/papers/6a76faade29fd788c9f6f7fa https://doi.org/10.1021/bi00459a026

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Implication

Saturation modulates acto-S1 ATP kinetics; extends in vitro cross-bridge models but leaves open physiological relevance in cardiac muscle.