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. Author manuscript; available in PMC: 2010 Jan 5.
Published in final edited form as: Biochemistry. 2009 Mar 17;48(10):2146–2155. doi: 10.1021/bi8019004

FIGURE 5.

FIGURE 5

Isoaffinity plot of all TGF-β2 and -β3 variants amenable to kinetic analysis. Each point represents the kinetic parameters derived from a single TβR-II dilution series over the indicated TGF-β variant surface. Key: TGF-β3(●), TGF-β2-TM (■), TGF-β2-K25R/K94R (▲), TGF-β3-R25K (○), and TGF-β3-V92I (×). All had their kinetic rate constants, ka and kd, determined by globally fitting their sensorgram data to a heterogeneous ligand model (BiaEvaluation v4.1). The rate constants associated with the higher affinity binding site (lowest KD) as determined by the heterogeneous ligand model were selected as the representative values for the interaction as previously determined (22).