A tabular representation of IRS-2 inhibition characteristics for the targeted serine proteases
Enzyme . | Amount of enzyme used, nM . | IRS2 IC50, nM . | IC50/enzyme ratio . | Inhibitor characteristics . |
---|---|---|---|---|
Cathepsin G | 12.2 | 11.5 ± 0.7 | 0.94 | Fast binding tight |
Chymase | 3.6 | 4 ± 0.2 | 1.11 | Slow binding tight |
Thrombin | 0.02 | 170.3 ± 11 | 8515 | Slow binding classical |
α-chymotrypsin | 0.038 | 0.38 ± 0.02 | 10 | N/A |
Trypsin | 0.25 | 562.7 ± 27.3 | 2251 | N/A |
Enzyme . | Amount of enzyme used, nM . | IRS2 IC50, nM . | IC50/enzyme ratio . | Inhibitor characteristics . |
---|---|---|---|---|
Cathepsin G | 12.2 | 11.5 ± 0.7 | 0.94 | Fast binding tight |
Chymase | 3.6 | 4 ± 0.2 | 1.11 | Slow binding tight |
Thrombin | 0.02 | 170.3 ± 11 | 8515 | Slow binding classical |
α-chymotrypsin | 0.038 | 0.38 ± 0.02 | 10 | N/A |
Trypsin | 0.25 | 562.7 ± 27.3 | 2251 | N/A |
The amount of enzyme used in the assays as well as the inhibitory concentration at half-maximum (IC50) of IRS-2 for these enzymes is stated in the first and second columns. The third column represents the ratio between IRS-2 IC50 and enzyme concentration, and the last column shows the binding characteristics of the inhibitor to the targeted enzymes with the relevance in host physiology (ie, tight or classical inhibitor, fast binding, or slow binding to the enzyme). Because trypsin and α-chymotrypsin were not physiologically relevant to our studies, we did not further study their inhibition characteristics, as depicted in by N/A.
NA indicates not applicable.