aptamer 15TBA RE19 RE21 RE23   55,2 ± 3,4 79,1 ± 2,6 168,9 ± 16,0 200,8 ± 16,5 aptamer RE25 RE27 RE29 RE31   294,1 ± 32,8 41,5 ± 2,1 28,3 ± 3,5 7,2 ± 2,5 Initial data were plotted as binding-curves, and linearized in Scatchard’s coordinates. The Kd increases in a row from RE19 to RE25 and then dramatically decreases (from RE27 to RE31). The Kd value characterizes the stability of the thrombin-aptamer complex.

Table 2: Apparent dissociation constants Kd (nM) of the thrombin-aptamer complexes (based on PAGE data).