Key result
Formation of an intramolecular or intermolecular disulfide bond in cardiac troponin C renders the protein Ca(2+)-independent in fast skeletal muscle myofibrils.
Population
Cardiac troponin C assayed in fast skeletal muscle myofibrils and cardiac myofibrils
Design
Preclinical
Authors
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Disulfide effects on troponin C unlikely to alter cardiac Ca²⁺ sensitivity; leaves open isoform-specific regulation in skeletal muscle.
Disulfide bond formation in cardiac troponin C constrains the protein into a conformation that mimics the Ca(2+)-bound form, rendering it Ca(2+)-independent in fast skeletal muscle myofibrils.
Putkey et al. (1993) studied this question. Formation of inter- and intramolecular disulfide bonds in cardiac troponin C was evaluated on Ca(2+)-independence in fast skeletal muscle myofibrils vs cardiac myofibrils. Formation of an intramolecular or intermolecular disulfide bond in cardiac troponin C renders the protein Ca(2+)-independent in fast skeletal muscle myofibrils.
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