Table 1

A tabular representation of IRS-2 inhibition characteristics for the targeted serine proteases

EnzymeAmount of enzyme used, nMIRS2 IC50, nMIC50/enzyme ratioInhibitor 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 
EnzymeAmount of enzyme used, nMIRS2 IC50, nMIC50/enzyme ratioInhibitor 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.

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