THE ACTION OF CRYSTALLINE PROTEOLYTIC ENZYMES ON ANGIOTONIN

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Abstract
Angiotonin was subjected to enzymatic digestion by crystalline carboxy-peptidase, chymotrypsin, trypsin, and pepsin. These enzymes were found to destroy it in vitro. Hydrogen ion optima and proteolytic coefficients for these reactions were determined and were found to be of approximately the expected magnitude for typical substrates. Regarding the purified crystalline enzymes as reagents, the experimental findings were interpreted on the basis of Bergmann's specificity studies. We were thus directed to the conclusion that angiotonin contains (1) a free terminal amino group, (2) a free terminal carboxyl group, (3) one basic amino acid residue which may be terminal but its carboxyl must be united in a peptide linkage, (4) one central dibasic amino acid residue in combination with an aromatic amino acid residue, (5) an aromatic amino acid residue which may be part of (4) and, if not part of (4) must be terminal with its carboxyl group in peptide linkage. The simplest compound satisfying these conditions is tyrosyl-arginylglutamyl-phenylalanine or a combination of amino acids with similar general characteristics.