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. 2021 Apr 28;296:100715. doi: 10.1016/j.jbc.2021.100715

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
a

Kinetic constants were obtained by fitting the data to a bivalent binding model.

b

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.

c

Calculated from equilibrium SPR measurements, in which Req was determined by fitting the association data to a pseudo first-order process to determine Req.

d

Six independent experiments were performed, and the values shown are the average ± SD.