December 1, 1981Journal of Biological ChemistryOpen Access

Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity.

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Population

Rabbit skeletal muscle Ca2+-binding subunit of troponin (TnC)

Design

Preclinical

Authors

ZGZenon GrabarekMassachusetts General Hospital WDW. DrabikowskiBoston Biomedical Research Institute PLPaul C. LeavisTufts University

Discussion

Member takes

Implication

No clinical implications from this animal study; leaves open whether mapped TnC sites inform human cardiac therapies.

Structured PICO

Population

Rabbit skeletal muscle Ca2+-binding subunit of troponin (TnC)

Intervention

Proteolytic fragments of TnC obtained by cleavage with trypsin, thrombin, and CNBr

Outcome

Ability to form binary and ternary complexes with TnI and TnT, and ability to replace TnC in reversing TnI inhibition of actomyosin ATPase activitysurrogate

This basic science study maps the specific binding regions of troponin C for troponin I and T, identifying the minimal fragment required to reverse TnI inhibition of actomyosin ATPase activity.

Cite This Study

Grabarek et al. (1981) studied this question.

synapsesocial.com/papers/6a202dbe6ed993cb49fbffd5 https://doi.org/10.1016/s0021-9258(18)43015-3

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Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider