The N-terminal amino acid residues of gelatin. 3. Enzymic degradation

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Abstract
Gelatin was degraded by pepsin, trypsin, chymotrypsin and papain. The N-terminal residues of the hydrolysates were determined by Sanger''s fluoro-dinitrobenzene technique. Attacks on similar peptide bonds are shown in all 4 cases, although to different degrees so far as observations from the amino end can discern. Papain, for example, attacks bonds involving alanine, and, to a lesser ex-tent, glycine, serine, threonine, aspartic acid and glutamic acid. The results are related to those of certain other workers using different proteins. It is suggested that proteolysis occurs in 2 ways; one involving a random breaking of peptide bonds, which closely follows the course of thermal degradation, the other in-volving a specific bond breaking action.