AN INHIBITOR OF CHYMOTRYPSIN FROM SOLANUM TUBEROSUM AND ITS BEHAVIOR TOWARD TRYPSIN

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Abstract
The isolation of a powerful inhibitor of chymotrypsin from white potatoes is described. It is a substance of protein-like nature, probably a polypeptide, unusually resistant to heat, acid, and alkali. It completely inhibits proteolysis, esterolysis, and milk clotting by chymotrypsin through the formation of an inactive enzyme-inhibitor complex. The complex has been prepared and again resolved into enzyme and inhibitor with nearly quantitative recovery of each. The inhibitor also forms a complex with trypsin and inhibits the proteolysis of casein by that enzyme. But no inhibitory activity has been noted against the tryptic scission of ester substrates of that enzyme. In view of the great variety of ester substrates of trypsin, all of which are split by "inhibited" trypsin, the hypothesis is advanced that at least in the case of trypsin the inhibitor does not involve the so-called "active center" directly.

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