Abstract
Summary
1. Using highly purified systems, no evidence was found that enterokinase overcomes the action of pancreatic trypsin inhibitor on trypsin. On the contrary, the inhibitor, after being exposed to the action of enterokinase, was quantitatively recovered, indicating that enterokinase neither formed a strong complex with the inhibitor, nor digested it. 2. It is tentatively suggested that the results which led to the postulation of the new activity of enterokinase could be explained by the assumption that the lipotropic fraction contained trypsinogen in addition to trypsin-trypsin inhibitor complex and free inhibitor.
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