TABLE 2.
Prethrombin 2 cleavage in the absence and presence of fragment 1.2
|
Constanta
|
Units
|
Measured
valueb
|
Sourcec
|
Fitted
termsd
|
|
|---|---|---|---|---|---|
| Fig. 5 | Fig. 6 | ||||
| Kd(P2·F12) | nm | 200 ± 10 | a | F | 165 ± 19 |
| n (mol F12/mol P2) | 0.90 ± 0.01 | a | F (1) | F (1) | |
| Kd(IIa·F12) | μm | 4.54 ± 0.3 | a | F | F |
| n (mol F12/mol IIa) | 0.93 ± 0.02 | a | F (1) | F (1) | |
| Ks(P2) | μm | 10.8 ± 0.6 | b | F | F |
| V/EP2 | s–1 | 2.62 ± 0.08 | b | F | F |
| Kp(IIa) | μm | 12.3 ± 0.3 | c | F | F |
| Ks(P2·F12) | nM | 176 ± 11 | d | 45.8 ± 6.3 | 158 ± 7 |
| V/EP2·F12 | s–1 | 76 ± 1 | d | 98 ± 4 | 114 ± 2 |
| Kd(E·P2,F12) | nm | 2.5 ± 0.4 | e | 0.7 ± 0.2 | 2.4 ± 0.4 |
| Kp(IIa·F12) | NDe | NF | NF | ||
| Kd(E·IIa,F12) | ND | NF | NF | ||
a
Symbolic constants correspond to those illustrated in Scheme 2
b
Measured values are presented ±95% confidence limits
c
Parameters are derived from isothermal titration calorimetry (a), derived from initial velocity studies (b), derived from product inhibition studies (c), taken from Orcutt and Krishnaswamy (12) (d), and calculated from Kd(P2·F12), Ks(P2), and Ks(P2·F12) (e)
d
Fitted terms are listed ±linear approximations of the 95% confidence limits. F denotes terms that were fixed using the measured values or fixed at the value indicated in parentheses. NF, not fitted
e
ND, not determined