Abstract
Since the report of Mizushima in which it was stated that a number of acidic anti-inflammatory drugs inhibited heat denaturation of protein, the interaction between anti-inflammatory agents and protein has been studied in various materials. F-1, a non-steroidal acidic analgesic and anti-inflammatory agent, was also investigated concerning the interaction with protein. F-i inhibited heat denaturation of bovin serum albumin (BSA) at pH 5.3 and the activity was more potent than that of phenylbutazone and similar to fenamates. F-i had a more potent inhibitory effect than phenylbutazone and fenamates on binding of pyridoxal-5-phosphoric acid and trinitrobenzaldehyde to BSA. Interaction of F-1 with the above BSA correlated with the inhibitory effect on hypotonic-hyperthermic hemolysis and enzyme activity of trypsin and α-chymotrypsin. F-1 showed a similar affinity to fenamates on erythrocytes in rats. Serum protein in adjuvant arthritis rats differed from control serum (decrease of albumin contents and A/G ratio, increase of haptoprotein and heat denaturation). F-1 improved qualitatively and quantitatively those serum changes. From the above results, F-1 was found to bind with protein and to have the same properties as known acidic antiinflammatory agents. Mode of interaction of F-1 differed to some extent from fenamates.
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