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J. Biol. Chem., Vol. 258, Issue 15, 9175-9177, Aug, 1983
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.
Kinetics of Ca2+ release shows interactions between the two classes of sites of troponin-C
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