Table 1. Thrombin inhibition kinetics by AT.
| Molecule | k(app)*10−3 (M−1s−1) | SI | k(assoc)*10−3 (M−1s−1) |
|---|---|---|---|
| AT | 3.3 ± 0.1 | 1.0 ± 0.1 | 3.3 ± 0.1 |
| AT + SOR | 2.6 ± 0.2 | 1.8 ± 0.1 | 4.7 ± 0.1 |
| AT + MANN | 2.7 ± 0.2 | 1.7 ± 0.1 | 4.6 ± 0.2 |
| AT + TRE | 2.9 ± 0.1 | 1.5 ± 0.2 | 4.4 ± 0.1 |
| AT + SER | 2.5 ± 0.2 | 2.1 ± 0.1 | 5.3 ± 0.1 |
| AT + TMAO | 2.3 ± 0.2 | 2.7 ± 0.2 | 6.2 ± 0.2 |
Apparent second-order rate constant (kapp), inhibition stoichiometries (SI) and second-order association rate constants (kassoc) of thrombin inhibition by AT in the absence and presence of small molecules. Observed pseudo-first-order rate constants, kobs were obtained from the negative slope of a plot of residual enzyme activity versus time (of thrombin and AT co-incubation). kapp were calculated by dividing kobs by molar concentration of AT. kassoc= kapp* S.I. Mean ± S.E.M. of three independent experiments is shown. Abbreviations: MANN, mannose; SER, serine; SOR, sorbitol; TMAO, trimethylamine N-oxide; TRE, trehalose.