February 1, 1990Journal of Biological ChemistryOpen Access

Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.

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Population

In vitro biochemical model (smooth muscle heavy meromyosin, actin, caldesmon)

Design

Preclinical

Authors

LVL VelazEast Carolina University RIRichard H. IngrahamMedical Council of Canada JCJoseph M. ChalovichEast Carolina University

Discussion

Member takes

Implication

Refines caldesmon's inhibitory mechanism on smooth muscle myosin; extends in vitro models but leaves open in vivo validation.

Structured PICO

Population

In vitro biochemical model (smooth muscle heavy meromyosin, actin, caldesmon)

Intervention

Digestion of caldesmon with chymotrypsin

Outcome

Actin-activated ATPase rate of smooth heavy meromyosin and binding of HMM.ATP to actinsurrogate

Caldesmon inhibits the actin-activated ATPase activity of smooth muscle heavy meromyosin by inhibiting the binding of the myosin-ATP complex to actin, with its myosin-binding region located at the amino terminus.

Cite This Study

Velaz et al. (1990) studied this question.

synapsesocial.com/papers/6a81e6ce2ac899ae0206e554 https://doi.org/10.1016/s0021-9258(19)39890-4

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Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider