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. 2014 Apr 21;289(22):15588–15601. doi: 10.1074/jbc.M113.535070

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© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Analysis of binding of rh-sCD157 to immobilized fibronectin and its proteolytic fragments by surface plasmon resonance. IAsys binding curves for the interaction of rh-sCD157 with full-length FN, HBD1, and HBD2 immobilized to the surface of a carboxymethyl dextran sensor. Increasing concentrations of rh-sCD157 were added to immobilized FN (A), HBD1 (B), or HBD2 (C), and their association was monitored over time. Binding of rh-sCD157 to FN, HBD1, and HBD2 was blocked by presaturating each protein with 1 mm heparin (*). D, sensorgrams obtained by probing immobilized CBD (top panel) or BSA (bottom panel) with rh-sCD157 at the indicated molarities. E, table of binding kinetics values (k_a, k_d, and K_D reported as the means ± S.E.) determined from the experimental curve fits.