Key result
The cloned salmonid cardiac troponin C exhibited a Ca2+-binding constant (K1/2 = 5.33 pCa units) within the range reported for the low-affinity sites of mammalian cTnC.
Population
Salmonid (Oncorhynchus mykiss and Salmo salar) cardiac troponin C cloned and expressed in Escherichia coli
Comparison
Cloning, sequencing, and expression of salmonid… vs Human/bovine/porcine cTnC isoforms
Design
Preclinical
Authors
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Findings from salmonid models warrant caution in extrapolating to mammalian cardiac regulation; leaves open the contribution of troponin interactions to myofibrillar Ca2+ sensitivity.
Despite striking differences in primary structure between salmonid and mammalian cardiac troponin C, the Ca2+ affinity of the low-affinity site is similar, suggesting that differences in intact myofibrillar Ca2+ sensitivity are likely influenced by interactions with other troponin proteins.
Moyes et al. (1996) studied this question. Cloning and expression of salmonid cardiac troponin C vs. Mammalian cTnC was evaluated on Ca2+-binding constant. The cloned salmonid cardiac troponin C exhibited a Ca2+-binding constant (K1/2 = 5.33 pCa units) within the range reported for the low-affinity sites of mammalian cTnC.
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