Key result
Cardiac TN-C undergoes a major conformational change upon binding Ca-2+ or Sr-2+ and reverses the inhibitory effect of skeletal TN-I on Mg-2+-activated ATPase.
Population
Purified cardiac muscle calcium-binding protein (TN-C) from bovine cardiac muscle
Comparison
Binding of Ca-2+, Sr-2+, or Mg-2+ vs Absence of Ca-2+ or exposure to different ions
Design
Preclinical
Authors
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Does not inform clinical care; leaves open translation of TN-C mechanisms from animal models to human disease.
This basic science study characterizes the biochemical and conformational properties of bovine cardiac TN-C, highlighting its structural response to calcium and strontium binding.
Burtnick et al. (1975) studied this question. Cardiac TN-C was evaluated on Molecular and biological properties. Cardiac TN-C undergoes a major conformational change upon binding Ca-2+ or Sr-2+ and reverses the inhibitory effect of skeletal TN-I on Mg-2+-activated ATPase.
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