TABLE 1.

Kinetic and equilibrium constants for the binding of RAP D1 and RAP D2 to LRP1

Kinetic data were derived by global fitting of the association and dissociation data to a 1:1 binding interaction. The experiments were performed in duplicate and values shown are averages ± S.E.

RAP fragment	ka	kd	t1/2	KDa
	m−1 s−1	s−1	s	nm
D1	7.65 ± 0.17 × 105	0.04 ± 0.004	17	53 ± 5
D2	1.58 ± 0.50 × 106	0.27 ± 0.06	2.5	238 ± 56

^a Data were determined from equilibrium measurements.