Table 1.

Comparison of the amount of bound antibody per molecule and binding site for Z_CaTriCys and Z_CaTetraCys on 1 ml columns. Coupling degrees in mg amino acid per ml matrix and M (Mw Z_CaTriCys: 23 036 Da, Z_CaTetCys: 30 675 Da), number of binding sites and the average amounts of IgG eluted with EDTA at pH 5.5 (n = 3) for Z_CaTriCys and Z_CaTetraCys. This data suggests that the tetrameric variant of Z_Ca has the highest binding performance.

		Coupling degree (mg amino acid/ml matrix)	Coupling degree (M)1	Molecules per column (mol)2	Binding sites per molecule3	Amount eluted IgG (mg)	Eluted IgG per molecule (mg/mol)4	Eluted IgG per binding site (mg/mol)5
ZCaTriCys	4.5		$2.0\ast {10}^{-4}$	2.0 * 10−7	3	3.6	1.8 * 107	6.0 * 106
ZCaTetraCys	3.2		$1.0\ast {10}^{-4}$	1.0 * 10−7	4	3.1	3.1 * 107	7.8 *106

¹ Coupling degree (mg/ml)/Molecular weight.² Coupling degree (M)*Column volume.³ Number of binding domains per multimer.⁴ Amount eluted IgG/Molecules per column.⁵ Amount eluted IgG/(Molecules per column*Binding sites per molecule).