Table 2.

Binding Constants for the Interaction of tPA and K2P With VSMCs

+/− 6AHAHigh AffinityLow Affinity
App. kdMax. Pln. Gen.App. kdMax. Pln. Gen.
(nmol/L)*(nmol/L)*
tPA − 25 ± 5 190 ± 30 300 ± 80 210 ± 25 
tPA ND ND 660 ± 90 135 ± 10 
K2P − ND ND 235 ± 45 140 ± 10 
K2P ND ND 810 ± 55 45 ± 5 
+/− 6AHAHigh AffinityLow Affinity
App. kdMax. Pln. Gen.App. kdMax. Pln. Gen.
(nmol/L)*(nmol/L)*
tPA − 25 ± 5 190 ± 30 300 ± 80 210 ± 25 
tPA ND ND 660 ± 90 135 ± 10 
K2P − ND ND 235 ± 45 140 ± 10 
K2P ND ND 810 ± 55 45 ± 5 

Binding constants derived from the data shown in Figs 5 and 6 are shown. Because of the functional nature of the binding assay, Bmax is equivalent to the maximum rate of plasmin generation by tPA (or K2P) bound to that site. By comparison, uPA binding to uPAR on these cells gives a maximum plasmin generation rate of 24 (±4) pmol/L⋅min−1 in the absence of 6AHA.

Abbreviation: ND, not detected.

*

Because the binding has not been formally shown to reach equilibrium under these experimental conditions, the parameter determined is not a true equilibrium constant and is thus referred to as an apparent kd.

Expressed as pmol/L⋅min−1.

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