Skip to main content
. 2020 May 15;11:913. doi: 10.3389/fmicb.2020.00913

TABLE 5.

Lipocalins-binding affinities towards apo- and ferric-ligands obtained using isothermal titration calorimetry (in TBS pH 7.4 at 30°C) in this study and compared values from the literature. Kd is the equilibrium dissociation constant, n the binding stoichiometry, ΔS the entropy, and ΔH the enthalpy.

Protein Ligands Reference Kd nM n ΔS cal/mol, K ΔH cal/mol
LCN2 apo-Ent This study 58.4 ± 12.5 0.872 −58.9 −2.78 × 104
Abergel et al., 2006 3.57
Fe3+-Ent This study 11.8 ± 8.8 0.863 −50.2 −2.62 × 104
Goetz et al., 2002 0.41
Fischbach et al., 2006 0.43
Li et al., 2015 240
Ex-FABP apo-Sal (or DGE) This study Under threshold
Fischbach et al., 2006 Under threshold
apo-Ent This study 86.2 ± 14.6 0.617 −60.9 −2.83 × 104
Correnti et al., 2011 0.5 ± 0.15
Fe3+-Ent This study 5.3 ± 3.8 0.672 −26.1 −1.94 × 104
Correnti et al., 2011 0.22 ± 0.06
apo-Sal (or DGE) This study Under threshold
Correnti et al., 2011 Under threshold
Cal-γ apo-Ent This study Under threshold
apo-Sal (or DGE) This study Under threshold
α-1-ovoglycoprotein apo-Ent This study Under threshold
apo-Sal (or DGE) This study Under threshold