Table 1.
Kinetic parameters of the interaction between pyrrolated BSA and apoE isoforms measured by surface plasmon resonance
ka, association rate constant; kd, dissociation rate constant; KD, equilibrium dissociation constant; Rmax, analyte binding capacity of the surface; χ2, measure of the average squared residual (the difference between the experimental data and the fitted curve); U value, estimate of the uniqueness of the calculated values for rate constants and Rmax.
ka | kd | KD | Rmax | χ2 | U value | |
---|---|---|---|---|---|---|
104 1/Ms | 10−5 1/s | 10−10 m | RU | RU2 | ||
apoE2 | 6.77 ± 0.63a | 8.17 ± 0.75 | 12.1 ± 0.57 | 22.7 ± 2.60 | 0.200 ± 0.144 | 14.0 ± 6.56 |
apoE3 | 8.74 ± 0.68 | 15.6 ± 4.71 | 18.1 ± 6.19 | 15.8 ± 2.43 | 0.245 ± 0.178 | 16.0 ± 9.54 |
apoE4 | 6.64 ± 0.24 | 15.2 ± 2.64 | 22.8 ± 3.80 | 25.4 ± 0.86 | 0.189 ± 0.056 | 4.67 ± 0.58 |
a The experiments were performed in triplicate, and the means ± S.D. are shown.