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. 2004 Sep;13(9):2437–2445. doi: 10.1110/ps.04762504

Table 1.

Equilibrium dissociation constants, Kd, measured at increasing SDS concentrations

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.