Abstract
The effect of mefenamic acid, flufenamic acid and of indomethacin on tryptic hydrolysis of bovine albumin (BA) and of the syn thetic substrates N-benzoyl-DL.-arginine-p-nitro anilide (BAPNA) and L-lysin-p-nitroanilide (LPA) was studied in vitro. Both fenamates and indomethacin inhibited tryptic hydrolysis of BA, indomethacin being more active. The failure of the tested antirheumatic drugs to inhibit BAPNA and LPA hydrolysis and the kinetics of BA decomposition showed that the binding of the antirheumatic drugs to the substrate (BA) is decisive for the inhibition of tryptic hydrolysis.
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