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. Author manuscript; available in PMC: 2012 Oct 3.
Published in final edited form as: Proteomics. 2011 Nov 23;11(24):4660–4676. doi: 10.1002/pmic.201100058

Figure 6.

Figure 6

Interaction between thrombospondin 1 and the NTD of α1(XI) collagen was analyzed by surface plasmon resonance. Collagen α1(XI) NTD was covalently coupled to the sensor chip, while thrombospondin 1 at concentrations ranging from 15 to 500 nM was allowed to bind to the Collagen α1(XI) NTD. The average of 3 runs to collect association data is shown. Using the data shown to fit to a steady state affinity model, the dissociation constant (Kd) was calculated to be 100nM for native thrombospondin 1, assuming a one-site association model.