Abstract
Summary
Trypsin in the absence of calcium is activated as much as 575% by nonsteroidal anti-inflammatory compounds when assayed with azocoll as substrate. Using a small synthetic compound, N-benzoyl-dl-arginine p-nitroanilide, as substrate much less activation was noted. Chymotrypsin was variably affected by less than 18% while no effect of the drugs was found on thrombin. Subtilisin was found to be inhibited slightly (less than 30%).
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