Fig. 6.
Fig. 6. Binding of HK or HKa to immobilized uPAR. / (A) The binding of HK or HKa (each 2 μg/mL) to immobilized suPAR or the truncated 2-domain uPAR (D2 + 3) (each 5 μg/mL) was studied in the absence (filled bars) or presence (hatched bars) of 50 μmol/L ZnCl2. Specific binding is shown as absorbance at 405 nm. Data are mean ± SEM (n = 3) of a typical experiment, and similar results were obtained in 3 separate experiments. (B) The binding of 2 μg/mL HKa together with 50 μmol/L ZnCl2 to immobilized suPAR was studied in the absence (−) or presence of 10 μg/mL heparin, 20 μg/mL VN, or 50 nmol/L uPA. Specific binding is expressed as absorbance at 405 nm. Data represent mean ± SEM (n = 3) of a typical experiment, and similar results were obtained in 3 separate experiments.

Binding of HK or HKa to immobilized uPAR.

(A) The binding of HK or HKa (each 2 μg/mL) to immobilized suPAR or the truncated 2-domain uPAR (D2 + 3) (each 5 μg/mL) was studied in the absence (filled bars) or presence (hatched bars) of 50 μmol/L ZnCl2. Specific binding is shown as absorbance at 405 nm. Data are mean ± SEM (n = 3) of a typical experiment, and similar results were obtained in 3 separate experiments. (B) The binding of 2 μg/mL HKa together with 50 μmol/L ZnCl2 to immobilized suPAR was studied in the absence (−) or presence of 10 μg/mL heparin, 20 μg/mL VN, or 50 nmol/L uPA. Specific binding is expressed as absorbance at 405 nm. Data represent mean ± SEM (n = 3) of a typical experiment, and similar results were obtained in 3 separate experiments.

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