TABLE 1.
Association and dissociation ratesa
| Complex | Result by BIAcore
|
Result by kinetic studies
|
|||
|---|---|---|---|---|---|
| Ka (M−1s−1) | Kd (s−1) | KD (nM) | IC50 (nM) | Ki (nM) | |
| PrKX–MBP-Rep52 | 2.4 × 104 ± 3 × 102 | 9 × 10−3 ± 8 × 10−5 | 385 | 210 | 90 |
| PrKX–MBP-Rep68Δ | 8.2 × 103 ± 2 × 102 | 1.8 × 10−2 ± 2 × 10−3 | 2,100 | ND | ND |
| PrKX–MBP-Rep78 | 1.5 × 104 ± 2 × 102 | 1 × 10−2 ± 1.2 × 10−4 | 680 | ND | ND |
| PKA–MBP-Rep52 | 6.5 × 103 ± 0.98 × 102 | 1.95 × 10−3 ± 2 × 10−5 | 320 | 340 | 330 ± 189 |
| PKA–MBP-Rep68Δ | NSBb | NSBb | NDc | NDc | NDc |
a
Association rate constants (Ka), dissociation rates (Kd), and binding constants (KD) were determined by SPR. IC50s were determined by in vitro kinase assays as described in Materials and Methods. Ki, IC50/(1 + [ligand/Kd]). Standard errors are given as standard deviations. ND, not determined.
b
NSB, no specific binding detected.
c
Because no specific binding was detected, value could not be determined.