TABLE 1.
Protein | Mean binding ± SDa |
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CXCR1 |
CXCR2 |
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Kon (M−1 s−1) | Koff (s−1) | Kd (nM) | Kon (M−1 s−1) | Koff (s−1) | Kd (nM) | |
SIV MA | (1.9 ± 0.5) × 105 | (4.2 ± 0.9) × 10−1 | 2,210 ± 723 | (2.0 ± 1.8) × 101 | (9.9 ± 0.05) × 10−6 | 495 ± 174 |
p17 | (1.3 ± 0.4) × 105 | (2.0 ± 0.5) × 10−1 | 1,538 ± 158 | (8.5 ± 0.1) × 104 | (1.0 ± 0.03) × 10−2 | 118 ± 5.3 |
The association rate (Kon) and the dissociation rate (Koff) are reported. The dissociation constant (Kd) was derived from the Koff/Kon ratio. The results are means of three independent experiments with similar results. The Kd values were also calculated independently from binding kinetics by performing a Scatchard plot analysis of the equilibrium binding data.