Table 1.
Kinetics for self-association of DnaK, KPf and PfHsp70-1.
| Ligand | Analyte | Ka (Ms−1) | Kd (1−1) | KD (M) | X 2 |
|---|---|---|---|---|---|
| DnaK | DnaK + ATP | 1.38 (±0.08) × 102 | 3.83 (±0.33) × 10−4 | 4.13 (±0.30) × 10−6* | 5.15 |
| DnaK | 1.27 (±0.07) × 103 | 6.51 (±0.01) × 10−2 | 4.67 (±0.27) × 10−5 | 4.21 | |
| DnaK + ADP | 1.22 (±0.13) × 102 | 6.49 (±0.09) × 10−3 | 4.60 (±0.09) × 10−5 | 5.41 | |
| KPf | KPf + ATP | 1.54 (±0.04) × 102 | 5.44 (±0.04) × 10−3 | 3.23 (±0.03) × 10−7* | 2.30 |
| KPf | 1.32 (±0.02) × 102 | 4.17 (±0.17) × 10−5 | 5.38 (±0.08) × 10−6 | 3.17 | |
| KPf + ADP | 1.42 (±0.02) × 102 | 5.23 (±0.03) × 10−3 | 4.65 (±1.5) × 10−5 | 2.37 | |
| PfHsp70-1 | PfHsp70-1 + ATP | 2.14 (±0.04) × 104 | 1.13 (±1.2) × 10−2 | 5.28 (±0.08) × 10−7* | 4.42 |
| PfHsp70-1 | 8.51 (±1.20) × 103 | 2.04 (±0.11) × 10−3 | 2.39 (±0.09) × 10−6 | 1.20 | |
| PfHsp70-1 + ADP | 1.00 (±0.17) × 102 | 1.71 (±0.07) × 10−4 | 1.71 (±0.10) × 10−6 | 4.45 |
The table shows the binding kinetics parameters of self-association of the three Hsp70s. The ligand fraction of each protein was the immobilized protein on the GLC chip surface, and the analyte fraction was injected at a flow rate of 50 μL/min. Self-association of the three proteins was investigated either in the absence or presence of ATP/ADP. Significant variation in KD values of data obtained in the presence of ATP was based on one-way ANOVA test (*p < 0.05).