Figure 5.
Figure 5. α2 Integrin I domain–mediated adhesion to SP-A and MBL. (A-B) Binding of the α2 integrin I domain (100 nM), E318A α2 integrin I domain mutant (100 nM), and GST (100 nM) to SP-A was measured in a solid-phase binding assay. Binding was determined in the presence of 2 mM MgCl2, 2 mM MnCl2, or 1 mM EDTA. (B) GST control was subtracted from experimental data. (C) Binding of the α2 integrin I domain (100 nM), E318A α2 integrin I domain mutant (100 nM), and GST (100 nM) to MBL was measured in a solid-phase binding assay. Binding was determined in the presence of 2 mM MgCl2 plus CaCl2 or 1 mM EDTA, as indicated. All results are presented as mean ± SEM from triplicate wells of a single experiment and represent 1 of at least 3 experiments demonstrating similar results. In all cases, at least 2 different preparations of purified I domain were used to verify that any results were not unique to a particular protein preparation.

α2 Integrin I domain–mediated adhesion to SP-A and MBL. (A-B) Binding of the α2 integrin I domain (100 nM), E318A α2 integrin I domain mutant (100 nM), and GST (100 nM) to SP-A was measured in a solid-phase binding assay. Binding was determined in the presence of 2 mM MgCl2, 2 mM MnCl2, or 1 mM EDTA. (B) GST control was subtracted from experimental data. (C) Binding of the α2 integrin I domain (100 nM), E318A α2 integrin I domain mutant (100 nM), and GST (100 nM) to MBL was measured in a solid-phase binding assay. Binding was determined in the presence of 2 mM MgCl2 plus CaCl2 or 1 mM EDTA, as indicated. All results are presented as mean ± SEM from triplicate wells of a single experiment and represent 1 of at least 3 experiments demonstrating similar results. In all cases, at least 2 different preparations of purified I domain were used to verify that any results were not unique to a particular protein preparation.

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