TABLE 1.

Dissociation constants and stoichiometries for the binding of HRG to γ_A /γ_A-fibrin(ogen), γ_A /γ′-fibrin(ogen), or γ′-peptide

The binding of HRG to immobilized fibrin(ogen) isoforms or γ′-peptide in the presence of 20 μm Zn²⁺ was quantified using SPR. K_d values were determined by kinetic analysis of the data, and stoichiometries were calculated according to the BIAtechnology handbook.

	Kd	Stoichiometry
	nm	HRG/molecule
γA/γA-Fibrinogen	8.8 ± 0.9	1.7 ± 0.3
γA/γ′-Fibrinogen	8.9 ± 3.9	3.2 ± 0.5
γA/γA-Fibrin	19.3 ± 2.6	1.8 ± 0.3
γA/γ′-Fibrin	10.9 ± 0.9	2.9 ± 0.6
γ′-Peptide	0.8 ± 0.01	0.7 ± 0.02