Fig. 5.
Fig. 5. Binding of radiolabeled α-defensin to isolated LRP. / (A) Binding of 125I-α-defensin to LRP-coated wells. Varying concentrations of 125I-α-defensin were added to LRP-coated wells in the presence or absence of excess unlabeled α-defensin, and the total (■) and specific (▪) binding were measured. (B) Inhibition of α-defensin binding by rRAP and anti-LRP antibodies. 125I-defensin (2 μM) was added to LRP-coated wells in the presence of medium alone (Cont) or medium supplemented with 20 nM rRAP (rRAP), anti-LRP antibody (anti-LRP), or irrelevant antibody (irAntib).

Binding of radiolabeled α-defensin to isolated LRP.

(A) Binding of 125I-α-defensin to LRP-coated wells. Varying concentrations of 125I-α-defensin were added to LRP-coated wells in the presence or absence of excess unlabeled α-defensin, and the total (■) and specific (▪) binding were measured. (B) Inhibition of α-defensin binding by rRAP and anti-LRP antibodies. 125I-defensin (2 μM) was added to LRP-coated wells in the presence of medium alone (Cont) or medium supplemented with 20 nM rRAP (rRAP), anti-LRP antibody (anti-LRP), or irrelevant antibody (irAntib).

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