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. 2001 Jan;12(1):73–83. doi: 10.1091/mbc.12.1.73

Table 1.

Modulation of Op18-tubulin binding affinities by phosphorylation and Glu-substitution of phosphorylation sites

Kd1 ± SE (μM) Kd2 ± SE (μM) Free [tubulin] at Half saturation of Op18 (μM)
Op18-wt 7.2  ± 1.9 0.9  ± 0.3 2.5
Op18-tetraE 27  ± 7.2 2.7  ± 1.3 8.8
Op18-wt-16,63-PO4 61  ± 23 2.9  ± 1.8 13.4

Equilibrium dissociation constants at pH 7.5 were calculated according to a two-site positive co-operativity model and are based on the data shown in Figure 3, A and B. The free tubulin concentration at half saturation was estimated from curves fitted according to a two-site cooperativity model.