Fig. 7

Determination of the binding affinity of SL1067 to IL-1α and the competition of IL-1α receptors with SL1067. a Shown is a four-parameter global fit (mean ± S.D., n = 4) of the relative fraction bound vs. IL-1α concentration. The mean (±S.D.) binding dissociation constant (K _d) determined from the four independent experiments is 7.3 ± 1.5 nM. b Displacement of radiolabeled SL1067 by unlabeled competitors SL1067 (open circles), IL-1 RI (open squares) or IL-1 RII (open triangles). Shown is a global fit (mean ± S.D., n = 3) to a one-site competition model of competitor concentration vs. fraction no competitor. The mean (±S.D.) inhibitory constants (K _i) from three determinations are: SL1067, K _i = 4.3 ± 1.5 nM; IL-1 RI K _i = 21 ± 9.8 nM and IL-1 RII K _i = 290 ± 130 nM