Protease inhibitors from Ascaris lumbricoides

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Abstract
An inhibitor of chymotrypsin was found in extracts of body wall of A. lumbricoides. It is inactivated by hot trichloroacetic acid and is therefore different from the trypsin inhibitor from the same source. Both substances inhibit esterase and proteinase activity stoichiometrically. The ester substrates temporarily block combination between enzyme and inhibitor; this observation is used to determine the rate constants for the combination. Both these inhibitors and several naturally occurring trypsin inhibitors were without effect on the activity of horse-liver esterase.