Table 2.

Relative affinities, μM, of the different mAbs with regard to series of Hb analogs, as determined by competitive EIA

mAb	Hb	9b	10b	12b	Ha	13b	11b	5b	5a	12a
PAR 2	3.3	ND	ND	36	186	ND	ND	750	4,200	ND
PAR 10	0.57	0.48	0.95	23	58	75	143	345	2,450	4,300
PAR 11	0.59	0.45	0.82	23.5	54.5	67	145	303	2,650	3,800
PAR 12	0.75	0.47	0.78	41	31	154	78	206	1,130	5,300
PAR 13	0.42	0.39	0.46	12	18	37	17	66	860	7,850
PAR 14	0.43	0.48	0.45	18	34	37.5	26	54.5	915	6,700
PAR 15	0.71	0.49	0.85	19	69	88	169	340	2,980	3,800
PAR 16	1.0	0.75	1.45	29	109	243.5	255	514	3,240	8,600
PAR 17	0.52	0.50	0.58	13	19.5	38	22	63	940	5,200
PAR 18	0.88	0.70	1.24	32	83	64	187	505	3,610	3,400
PAR 19	0.76	0.60	0.82	37	37	120	95	209	1,140	9,700
PAR 20	1.02	0.51	0.84	58.5	38	126	118	332	1,370	5,550
PAR 21	0.56	0.25	0.88	26	18.5	154	79	219	1,480	6,800

Results are expressed in terms of B/Bo (50%) (see Materials and Methods). Because 12a and 13b are AChE inhibitors (IC₅₀ = 2.7 ± 0.3 μM and IC₅₀ = 48 ± 5 μM), affinity was determined by two-step competitive ELISA and not by EIA, in order to prevent the simultaneous presence in the assay of AChE and its unbound inhibitors. ND, not determined.