TABLE 3.
Binding data from isothermal titration calorimetry
The intermolecular interactions of the indicated ligands were measured as described under “Experimental Procedures” and illustrated in Fig. 7. Fg, fibrinogen; Plg, plasminogen; N, size of binding site (in number of nucleotides when DNA is the binding partner or number of molecules when histone is used); Kd, dissociation equilibrium constant; ΔH, enthalpy change. Mean and S.D. of at least four measurements are shown.
| FDP/DNA |
FDP/histone |
Fg/DNA |
Plg/DNA |
|||||
|---|---|---|---|---|---|---|---|---|
| Mean | S.D. | Mean | S.D. | Mean | S.D. | Mean | S.D. | |
| N | 1315.8 | 136.3 | 1.6 | 0.5 | 2145.9 | 1903.0 | 682.0 | 110.9 |
| Kd (nm) | 136.1 | 111.7 | 190.7 | 91.7 | 534.3 | 52.8 | 524.1 | 72.7 |
| ΔH (kcal/mol) | −239.5 | 28.8 | −12.8 | 2.9 | −1116.3 | 1874.4 | −153.0 | 135.6 |