Inhibition of enzymes by alkylsalicylic acids

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Abstract
5-n-Alkylsalicylates inhibited a variety of enzymes that transform acidic substances, viz. glucose-6-phosphate dehydrogenase, glyoxalase, xanthine oxidase, carbonic anhydrase and D-amino-acid oxidase. Inhibitory potency rose to a peak at the n-nonyl derivative. None of the tests were of value, either singly or in combination, as screening processes for anti-inflammatory activity. The comparable results with a trinitrobenzaldehyde reagent suggest that the various inhibitions arise by non-specific association of the drugs with arginine and lysine residues in proteins.