Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides

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Abstract
The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mold [Penicillium janthinellum] acid protease, penicillopepsin (EC 3.4.23.7) were determined. These peptides established the sequences of 26 unique fragments of up to 28 residues in length. The 28-residue fragment was identified as the N-terminal region. The C-terminal region is represented by a 13-residue fragment. The amino acids contained in these fragments account for about 85% of the residues of the enzyme.