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. Author manuscript; available in PMC: 2019 May 31.
Published in final edited form as: Biochemistry. 2017 May 2;56(19):2518–2528. doi: 10.1021/acs.biochem.7b00087

Table 2.

ELISA- and SPR-Determined Equilibrium Dissociation Constants (Kd) for the Interaction of the Fibrin-Binding VLDLR(1–8) Fragment with the Recombinant and Synthetic Fragments of Fibrin βN-Domains.

β N-fragments Kd (nM)a
ELISA SPR
(β 15–66)2 fragment     3.6 ± 0.8    3.1 ± 0.2
β 15–64 fragment     n.d.b    6.1 ± 1.6 μ M
(β 15–44)2 fragment     n.d.b    67 ± 9 μ M
Ionic Strength Dependence
(β 15–66)2 + 0.15 M NaCl     3.0 ± 0.1    3.1 ± 0.2
(β 15–66)2 + 0.2 M NaCl     6.0 ± 0.3    5.8 ± 0.2
(β 15–66)2 + 0.25 M NaCl     13.5 ± 1.3    11.1 ± 0.1
(β 15–66)2 + 0.3 M NaCl    34.1 ± 1.9    20.5 ± 2.7
a

All Kd values are in nM except those for the β15–64 and (β15–44)2 fragment, which are presented in μM.

b

Not detected due to low binding signal.