In Vitro Action of a New Lipotropic Fraction in the Pancreas

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Abstract
A highly lipotropic pancreatic fraction (A-1), without demonstrable direct proteolytic activity, has been studied in vitro. It contains an active proteolytic enzyme tentatively identified as trypsin, combined with an excess of an enzyme inhibitor, tentatively identified as pancreatic trypsin inhibitor. The action of the inhibitor may be overcome by addition of a substance present in duodenal juice and presumed to be enterokinase. This action of enterokinase has not been previously noted. It is assumed that the lipotropic activity of fraction A-I is based on enzymatic liberation of methionine from ingested protein, after the activation of the proteolytic enzyme in the intestine. The use of a microbiol. assay for methionine is described as a method of testing enzyme activity. An arbitrary unit, the (TU) meth, is defined as the no. of [mu]g. of methionine released/hr./[mu]g. of enzyme.
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