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. Author manuscript; available in PMC: 2009 Jan 30.
Published in final edited form as: Biochemistry. 2008 Apr 15;47(18):5111–5126. doi: 10.1021/bi702537s

Table 1.

Dissociation Constants for Ca2+ Binding to S100A4

[EF1] (μM) [EF2] (μM)
S100A4 (low salt) 54.4 ± 10.8a 3.3 ± 1.3a
S100A4 (high salt) >500b 2.6 ± 1.3b
S100A4 and MIIA1851–1960 (high salt) 3.6 ± 0.2c 0.26 ± 0.01c
a

The dissociation constants for Ca2+ binding to each S100A4 EF-hand domain were determined by ITC under low-salt conditions [20 mM Tris (pH 7.5), 20 mM KCl, and 250 μM TCEP].

b

These values are from published studies (71). The dissociation constants for Ca2+ binding to each S100A4 EF-hand domain were determined using a 5,5′Br2-BAPTA competition assay under high-salt conditions [20 mM Tris (pH 7.5), 150 mM KCl, 1 mM DTT, and 0.02% NaN3].

c

The dissociation constants for Ca2+ binding to each S100A4 EF-hand domain in the presence of MIIA1851–1960 were determined using a 5,5′Br2-BAPTA competition assay under high-salt conditions [20 mM Tris (pH 7.5), 150 mM KCl, 1 mM DTT, and 0.02% NaN3].