Functional characterization of the PS mutants
. | C4BP . | HPS54 . | PC/PS/PE vesicles . |
|---|---|---|---|
| Wild-type rPS | 4.4 ± 0.7 | 1.6 ± 0.3 | 9.0 ± 0.5 |
| GlaFII-ΔTSR-PS | 11.4 ± 1.3 | 1.1 ± 0.2 | 17.0 ± 0.9 |
| GlaFII-PS | 2.6 ± 0.2 | 1.4 ± 0.3 | 21.1 ± 1.5 |
| F1FII-GlaPS-PS | 2.4 ± 0.3 | 1.4 ± 0.2 | 84.8 ± 3.4 |
| F2FII-GlaPS-PS | 5.9 ± 0.4 | 5.0 ± 1.7 | 9.5 ± 1.1 |
| F12PS-GlaFII-PS | 1.6 ± 0.2 | 3.6 ± 0.6 | 8.6 ± 0.8 |
. | C4BP . | HPS54 . | PC/PS/PE vesicles . |
|---|---|---|---|
| Wild-type rPS | 4.4 ± 0.7 | 1.6 ± 0.3 | 9.0 ± 0.5 |
| GlaFII-ΔTSR-PS | 11.4 ± 1.3 | 1.1 ± 0.2 | 17.0 ± 0.9 |
| GlaFII-PS | 2.6 ± 0.2 | 1.4 ± 0.3 | 21.1 ± 1.5 |
| F1FII-GlaPS-PS | 2.4 ± 0.3 | 1.4 ± 0.2 | 84.8 ± 3.4 |
| F2FII-GlaPS-PS | 5.9 ± 0.4 | 5.0 ± 1.7 | 9.5 ± 1.1 |
| F12PS-GlaFII-PS | 1.6 ± 0.2 | 3.6 ± 0.6 | 8.6 ± 0.8 |
All values are expressed as Kd app, nM.
Binding of wild-type rPS and PS mutants to immobilized C4BP, immobilized mAb HPS54, and immobilized phospholipid vesicles (PC/PS/PE vesicles) was evaluated as described in “Materials and methods.” Binding curves yielded the Kd app values, using nonlinear regression analysis of the A490 value as a function of the PS concentration.