Table 1.

Kinetic analysis of 16D11 hu-mAb interaction with rHAs from PR8, Hokkaido and Memphis influenza viruses.

	Ka (mean ± SD) M−1 s−1	Kd (mean ± SD) s−1	KD nM	t1/2 min
PR8/A/34	$(22.4\pm 0.2)\times 10^3$	$(4.39\pm 0.03)\times {10}^{-3}$	199	2.62
Hokaido	$(25.8\pm 0.2)\times {10}^3$	$(3.32\pm 0.03)\times {10}^{-3}$	130	3.46
Memphis	n.b.d*	n.b.d	n.b.d	N/A

SPR sensograms for the interaction of 16D11 with rHA proteins as shown in Figure 7. The kinetic data were fit using a 1:1 Langmuir binding model for the estimation of the association (ka) and dissociation (kd) rates and affinity (KD=ka/kd). No binding was detected (*nbd.) for the interaction of 16D11 with rHA of Memphis virus. The complex half-life was calculated as t^1/2 = Ln/kd.