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. Author manuscript; available in PMC: 2011 Nov 30.
Published in final edited form as: Biochemistry. 2011 Jul 13;50(32):6920–6932. doi: 10.1021/bi200498q

Table 2.

Dissociation Constantsa for Binding of Ca2+ to S100A4

protein MIIA1851–1960 EF1 (μM) EF2 (μM)
wt-S100A4b + 4.26 ± 0.04 0.44 ± 0.04
wt-S100A4c >500 7.6 ± 0.4
sc-S100A4–5b + 1.65 ± 0.05 0.74 ± 0.11
sc-S100A4–10b + 3.20 ± 0.30 1.10 ± 0.18
sc-S100A4–5M1b + 169 ± 23 0.51 ± 0.05
sc-S100A4–5M1c 366 ± 93 1.83 ± 0.34
sc-S100A4–5M2b + 205 ± 41 0.24 ± 0.03
sc-S100A4–5M2c >500 0.75 ± 0.21
sc-S100A4–10M1b + 244 ± 46 0.43 ± 0.06
sc-S100A4–10M1c 223 ± 26 1.46 ± 0.31
sc-S100A4–10M2b + >500 0.92 ± 0.30
sc-S100A4–10M2c >500 1.26 ± 0.12
a

Values represent the average from two or three independent experiments.

b

Macroscopic Ca2+ binding constants determined for 12.5 μM S100A4 dimer in the presence of 100 μM MIIA1851–1960 monomer.

c

Macroscopic Ca2+ binding constants determined for 12.5 μM S100A4 dimer in the absence of target.