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. 2009 May 12;284(28):19090–19100. doi: 10.1074/jbc.M109.007021

FIGURE 1.

FIGURE 1.

The actin-Tm-activated myosin ATPase activity of HCM cTnC mutants as a function of pCa. A, HcTnC mutant or WT at 100%. B, HcTnC mutants and WT at a 50% to 50% ratio. The experiments were performed using 0.6 μm myosin, 3.5 μm actin, 1 μm Tm, and 1 μm preformed Tn complex. The buffer conditions were as described under “Experimental Procedures.” The basal ATPase activity at pCa 8.0 was considered 0%. The intermediate points were normalized to the maximal ATPase activity at pCa 4.0 and were considered 100%. The specific ATPase activity at pCa 8.0 was 0.15, 0.19, 0.11, 0.19, and 0.18 mol of Pi × mol of myosin−1 × s−1 for WT, A8V, C84Y, E134D, and D145E, respectively. Each curve represents an average of six to seven experiments, and error is reported as mean ± S.E.

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