Table 3.
Binding and activation of PKG Iα constructs
The data are represented as the mean ± S.D. —, not measured.
| PKG Iα construct | cNMP | Binding (SPR) |
Activation (32PO4 assay) |
||||||
|---|---|---|---|---|---|---|---|---|---|
| One-site model |
Two-site model |
||||||||
| KD | nH | KDHi | KDLo | N | Ka | nH | N | ||
| μm | μm | μm | μm | ||||||
| Full length | cGMP | 7.9 ± 1.1 | 0.60 ± 0.04 | 1.6 ± 0.3 | 90.2 ± 33.9 | 6 | 0.182 ± 0.004 | 1.58 ± 0.06 | 12 |
| Full length | cAMP | 387 ± 37 | 0.76 ± 0.03 | 51.7 ± 25.4 | 685 ± 174 | 5 | 10.80 ± 0.67 | 1.75 ± 0.09 | 6 |
| Δ53 | cGMP | 2.9 ± 0.4 | 0.74 ± 0.06 | 1.0 ± 0.4 | 19.1 ± 16.7 | 6 | 0.250 ± 0.010 | 0.97 ± 0.03 | 5 |
| Δ53 | cAMP | 297 ± 21 | 0.76 ± 0.03 | 36.6 ± 9.2 | 509 ± 62 | 4 | 0.860 ± 0.157 | 0.81 ± 0.06 | 6 |
| 1–326 | cGMP | 21.3 ± 1.3 | 0.81 ± 0.03 | 8.4 ± 2.5 | 74.4 ± 38.6 | 6 | — | — | |
| 1–326 | cAMP | 64.3 ± 5.3 | 0.72 ± 0.03 | 16.9 ± 3.9 | 312 ± 112 | 4 | — | — | |
| 78–326 | cGMP | 30.0 ± 1.1 | 0.90 ± 0.02 | 3.2 ± 3.1 | 35.5 ± 4.4 | 6 | — | — | |
| 78–326 | cAMP | 340 ± 10 | 0.92 ± 0.02 | 4.8 ± 3.1 | 350 ± 10 | 4 | — | — | |