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. 2002 Feb;128(2):714–725. doi: 10.1104/pp.010531

Figure 6.

Figure 6

Scatchard plots of ABA-binding activities to the crude (a) and purified (b) proteins. B, 3H-ABA bound; F, 3H-ABA free. For the crude proteins (a), all points except for the first two were fitted with a linear relationship (r2 = 0.98), and according to the Scatchard plot, the maximum binding activity (Bmax) and the equilibrium dissociation constant (Kd) were calculated: Bmax = 68 nmol g−1 protein and Kd = 19 nm. The fitted relationship of the purified protein (b) was also linear (r2 = 0.99) with Bmax = 0.87 mol mol −1 protein and Kd = 21 nm. Points represent the means ± sd of five determinations.