Table 1.
SDS (μM) | Kd (μM) | Kdapp* (μM) |
0 | 3.1 ± 0.3 | 8.2 |
50 | 6.3 ± 0.6 | 17.8 |
100 | 16.2 ± 1.6 | n.d. |
250 | n.d. | |
500 | n.d. | |
1000 | n.d. |
Equilibrium dissociation constants, Kd, obtained by fluorescence titrations of β-DG(654–750) with a synthetic peptide α-DG(549–567) (central column, standard errors are reported) and by solid-phase binding assays of biotinylated β-DG(654–750) with Trx-α-DG(485–600) (right column), carried out in the presence of increasing SDS concentrations. (*) Apparent equilibrium dissociation constants. Kd values represent an average of three independent experiments. (n.d.) Not determined.