TABLE 2.
Affinity of cleaved PAI-1 for different (CR)2 and (CR)3 fragments
| CR fragmenta |
|||||||||
|---|---|---|---|---|---|---|---|---|---|
| CR34 | CR45 | CR56 | CR78 | CR89 | CR345 | CR456 | CR567 | CR678 | |
| Kd (nm) | 62 ± 15 | 18 ± 6 | 48 ± 18 | 90 ± 13 | 1200 ± 200 | 22 ± 4 | 2.7 ± 0.5 | 32 ± 10 | 59 ± 5 |
| ΔG0 (kJ mol−1) | −41.1 ± 0.6 | −44.1 ± 0.9 | −41.7 ± 1 | −40.1 ± 0.4 | −33.7 ± 0.5 | −43.6 ± 0.5 | −48.8 ± 0.5 | −42.7 ± 0.8 | −41.2 ± 0.2 |
| ΔFmax/F0b | 0.53 | 0.53 | 0.22 | 0.50 | 0.24 | 0.48 | 0.55 | 0.28 | 0.26 |
aKd values are the average and spread of best fits to multiple independent determinations.
bΔFmax/F0 is the change in fluorescence intensity at saturation relative to the starting fluorescence intensity of the (CR)x species, measured at the wavelength of observation.