Abstract
Summary
Treatment of trypsin with chlorambucil in the absence of calcium ion results in an enzyme incapable of hydrolyzing p-toluene-sulfonyl-l-arginine methyl ester. Similar treatment of trypsinogen destroys potential tryptic activity. Calcium ion affects a protective influence on the enzyme and zymogen in the presence of chlorambucil by maintaining the enzymic activity of trypsin, and by preserving much of the potential activity of the zymogen. It is suggested that chlorambucil may affect physiological activity by reacting, in part, with the primary carboxyl binding site in trypsin and trypsinogen.
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