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. 2006 Sep 8;103(38):13991–13996. doi: 10.1073/pnas.0605716103

Fig. 1.

Fig. 1.

SPR analysis of binding by the αL I domains to Abs AL-57 and MHM24. The HA (K287C/K294C), IA (L161C/F299C), or low-affinity WT I domain was perfused onto immobilized Abs in the presence of 1 mM MgCl2 (A) or 10 mM EDTA (B). The concentration series for MHM24 was 3.91, 7.81, 15.63, 31.25, 62.5, 125, 250, and 500 nM. For AL-57, the concentration series was 15.6, 31.3, 62.5, 125, and 250 nM for the HA I domain and 31.25, 62.5, 125, 250, and 500 nM for WT and IA I domains. In all cases, higher concentrations gave higher responses (except that differences are not visible for WT with AL-57 in Mg2+ and for HA with AL-57 in EDTA).