Table 1.
Equilibrium binding parameters for SK constructs binding to 5-fluorescein-labeled [Lys]Pga
| SK construct | No 6-AHA
|
10 mM 6-AHA
|
||
|---|---|---|---|---|
| Kd (nM) | ΔFmax/Fo (%) | Kd (nM) | ΔFmax/Fo (%) | |
| Native SK | 23 ± 6b | −22 ± 1 | 310 ± 60 | −22 ± 1 |
| SK-His6 | 240 ± 30 | −33 ± 1 | 290 ± 50 | −24 ± 1 |
| SKΔ (R253-L260) ΔK414-His6 | 470 ± 40 | −26 ± 1 | 820 ± 90 | −22 ± 1 |
a
Dissociation constants (Kd) and maximum fluorescence changes (ΔFmax/Fo) are listed for the titrations shown in Fig. 5. [5F]FFR-[Lys]Pg (15 nM) was titrated with the indicated SK constructs in the absence (No 6-AHA) and presence of 6-AHA (10 mM 6-AHA). Binding experiments were performed and analyzed as described in Materials and methods.
b
Experimental error represents the 95% confidence interval.