Table 1.
Kinetica and equilibrium constants for the binding of lipid-free apoE isoforms to LRP1
Protein | ka1 (M−1 s−1) | kd1 (1/s) | ka2 (1/s) | kd2 (1/s) | bKD (nM) | cKD (nM) |
---|---|---|---|---|---|---|
dApoE2 | 3.4 ± 0.4 × 104 | 8.6 ± 0.5 × 10−2 | 1.0 ± 0.2 × 10−2 | 2.8 ± 0.4 × 10−3 | 529 ± 75 | 493 ± 86 |
dApoE3 | 4.3 ± 0.8 × 104 | 9.0 ± 0.7 × 10−2 | 9.6 ± 0.1 × 10−3 | 2.6 ± 0.2 × 10−3 | 456 ± 48 | 398 ± 67 |
dApoE4 | 6.2 ± 0.7 × 104 | 6.5 ± 0.4 × 10−2 | 9.9 ± 0.3 × 10−3 | 2.7 ± 0.3 × 10−3 | 202 ± 51 | 236 ± 101 |
Kinetic constants were obtained by fitting the data to a bivalent binding model.
The equilibrium binding constant KA was calculated using the following equation: KA = (ka1/kd1) ∗ (1 + (ka2/kd2)), and KD was calculated as: KD = 1/KA.
Calculated from equilibrium SPR measurements, in which Req was determined by fitting the association data to a pseudo first-order process to determine Req.
Six independent experiments were performed, and the values shown are the average ± SD.