Table 1.
Effects of CDSO3 on the Michaelis–Menten Parameters of Thrombin and Various Substratesa
[CDS03] (nM) | Substrate | Km (μM)b | Vmax (mAU/min)b |
---|---|---|---|
0 | Spectrozyme TH | 2.2 ± 0.2 | 21 ± 0.7 |
30 | ” | 1.3 ± 0.1 | 15 ± 0.3 |
105 | ” | 1.2 ± 0.1 | 11 ± 0.3 |
300 | ” | 0.85 ± 0.1 | 9.5 ± 0.2 |
0 | S-2238 | 1.3 ± 0.1 | 10.4 ± 0.2 |
1 | ” | 1.3 ± 0.2 | 8.8 ± 0.2 |
10.5 | ” | 1.1 ± 0.2 | 6.2 ± 0.2 |
30 | ” | 1.4 ± 0.3 | 5.0 ± 0.2 |
105 | ” | 1.2 ± 0.3 | 4.6 ± 0.2 |
0 | Spectrozyme FXa | 61 ± 3 | 36 ± 0.6 |
10.5 | ” | 42 ± 4 | 31 ± 0.8 |
30 | ” | 40 ± 5 | 23 ± 0.9 |
105 | ” | 40 ± 5 | 18 ± 0.7 |
203 | ” | 39 ± 10 | 12 ± 1 |
0 | Spectrozyme Pro | 1.3 ± 0.2 | 36 ± 1 |
30 | ” | 0.5 ± 0.05 | 23 ± 0.3 |
120 | ” | 0.7 ± 0.1 | 21 ± 0.5 |
0 | Spectrozyme PCa | 4.5 ± 0.5 | 107 ± 3 |
30 | ” | 7.3 ± 2.0 | 82 ± 4 |
90 | ” | 9.1 ± 3.2 | 67 ± 5 |
KM and VMAX values of substrate hydrolysis by human thrombin were measured as described in Experimental Procedures. mAU indicates milliabsorbance units.
Error represents ±1 SE.