Pepsin is one of the main proteolytic enzymes secreted by the gastric mucosa. Pepsin consists of a single polypeptide chain and arises from its precursor, pepsinogen, by removal of a 41 amino acid segment from the N-terminus. Pepsinogen is synthesized in the stomach lining, and hydrochloric acid, also produced by the gastric mucosa, is necessary to convert the inactive enzyme and to maintain the optimum acidity (pH 1-3) for pepsin function. Pepsin is particularly effective in cleaving peptide bonds involving aromatic amino acids. Pepsin shows extremely broad specificity, and although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. The amino acid composition of Pepsin C differs from those of pepsinogen and pepsin especially in the content of basic amino acids, glutamic acid, aspartic acid, leucine and isoleucine.

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