Table 1.
Binding constants for the BSA-ANS interaction in buffer and the ATPS at different pressures (T = 25 °C).
| Solvent | Buffer | ATPS | ATPS |
|---|---|---|---|
| p/bar | aKb/M−1 106 | bKb1/M−1 106 | cKb2/M−1 106 |
| 1 | 4.2 ± 0.9 | 4.3 ± 2.0 | 0.42 ± 0.22 |
| 500 | 3.2 ± 1.1 | 5.4 ± 2.5 | 0.23 ± 0.12 |
| 1000 | 2.8 ± 0.9 | 0.41 ± 0.20 | 0.22 ± 0.12 |
| 1500 | 1.9 ± 0.6 | 0.82 ± 0.40 | 0.090 ± 0.045 |
| 2000 | 1.2 ± 0.4 | 0.40 ± 0.21 | 0.099 ± 0.050 |
aThe binding stoichiometry for BSA:ANS is 1:3 at each pressure; bTwo sites were assigned for this class with stoichiometry 1:2 BSA:ANS; cOne site was assigned to this class with stoichiometry 1:1 BSA:ANS.