Table 5.
Rate constants used in the CC model (see Jones and Mann, 1994).
| Value | Units | Description | |
|---|---|---|---|
| k1 | 2e4 | mol−1 m3 s−1 | Activation of V by Xa (2nd order) |
| k2 | 2e4 | mol−1 m3 s−1 | Activation of V by IIa (2nd order) |
| k3 | 1e4 | mol−1 m3 s−1 | Activation of VIII by Xa (2nd order) |
| k4 | 2e4 | mol−1 m3 s−1 | Activation of VIII by IIa (2nd order) |
| k5 | 1e4 | mol−1 m3 s−1 | Conversion of mIIa to IIa by Va:Xa (2nd order) |
| k6 | 1e5 | mol−1 m3 s−1 | On-rate for rapidly formed complexes (2nd order) |
| k7 | 1e4 | mol−1 m3 s−1 | On-rate for the VIIIa:IXa complex (2nd order) |
| k8 | 4e5 | mol−1 m3 s−1 | On-rate for the Va:Xa complex (2nd order) |
| k9 | 0.005 | s−1 | Off-rate for VIIIa:IXa complex |
| k10 | 0.4 | s−1 | Off-rate for Va:Xa complex |
| k11 | 0.3 | s−1 | Vmax for activation of IX by TF:VIIa (Michaelis–Menten kinetics) |
| k12 | 1.15 | s−1 | Vmax for activation of X by TF:VIIa (Michaelis–Menten kinetics) |
| k13 | 8.2 | s−1 | Vmax for activation of IX by VIIIa:IXa (Michaelis–Menten kinetics) |
| k14 | 32 | s−1 | Vmax for mIIa formation by Va:Xa (Michaelis–Menten kinetics) |
| k15 | 1e2 | mol−1 m3 s−1 | Activation of IX by Xa (2nd order) |
| k16 | 24 | s−1 | Off-rate for IX on TF:VIIa complex |
| k17 | 44 | s−1 | Off-rate for X on TF:VIIa complex |
| k18 | 0.001 | s−1 | Off-rate for X on VIIIa:IXa complex |
| k19 | 70 | s−1 | Off-rate for II on Va:Xa complex |
Michaelis–Menten kinetics (Metiu, 2006) models enzyme kinetics.