. Author manuscript; available in PMC: 2009 Aug 7.

Published in final edited form as: J Control Release. 2008 May 1;129(3):179–186. doi: 10.1016/j.jconrel.2008.04.021

Table 1.

Surface Plasmon Resonance Data for Antagonist Binding to Immobilized TNFα

Antagonist	k_on (10⁴ M⁻¹ s⁻¹)	k_off (10⁻⁴ s⁻¹)	K_D (nM)	K_D/K_D,sTNFRII
sTNFRII	4.5 ± 0.5	0.22 ± 0.08	0.47 ± 0.12	1
ELP-sTNFRII (ITC purified)	1.4 ± 0.6	10 ± 6^*	73 ± 12^*	153
ELP-sTNFRII (Unfolded)	0.12 ± 0.08	5 ± 2^*	470 ± 180^*	989
ELP-sTNFRII (refold mixture)	0.7 ± 0.4	1.1 ± 0.4^*	17 ± 8^*	35
ELP-sTNFRII (immunoprecipitated)	4.4 ± 1.8	1.6 ± 0.7^*	3.5 ± 0.3^*	7
ELP-sTNFRII (TNFα-affinity purified)	4.6 ± 1.8	0.9 ± 0.2^*	2.1 ± 0.9^*	4.5
ELP	0.013 ± 0.018^#	42 ± 39	7400 ± 400^#	150000

k_on – association rate constant

k_off – dissociation rate constant

K_D – equilibrium dissociation constant

values for ELP-sTNFRII are significantly different from values for sTNFRII at p < 0.05

values for ELP are significantly different from values for both sTNFRII and ELP-sTNFRII at p < 0.05