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J. Biol. Chem., Vol. 258, Issue 15, 9175-9177, Aug, 1983

Kinetics of Ca2+ release shows interactions between the two classes of sites of troponin-C

CL Wang, PC Leavis and J Gergely

The kinetics of Ca2+-release from the two high affinity sites of troponin-C (TnC) was studied by the stopped flow technique following rapid mixing with either EDTA or excess TbCl3. The rate constants obtained by the two methods were 2.8 and 0.7 s-1, respectively. For the tryptic fragment of TnC that contains only the COOH-terminal half of the molecule, both methods generate rate constants of 2.2 s-1. These results are consistent with the interpretation that binding of Tb3+ to the Ca2+-specific sites reduces the rate of dissociation of Ca2+ from, and thereby enhances the affinity for, the Ca2+-Mg2+ sites; this, in turn, suggests interactions between the two halves of the TnC molecule.
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J.-M. Francois, Z. Sheng, D. Szczesna, and J. D. Potter
The Functional Role of the Domains of Troponin-C Investigated with Thrombin Fragments of Troponin-C Reconstituted into Skinned Muscle Fibers
J. Biol. Chem., August 18, 1995; 270(33): 19287 - 19293.
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