title: Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides.
abstract: The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mould acid protease, penicillopepsin (EC 3.4.23.7), have been 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 some 85% of the residues of the enzyme.
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002918:Chymotrypsin; D010450:Endopeptidases / Q000378:metabolism; D010406:Penicillins; D010407:Penicillium / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis*
chemical_list: D010406:Penicillins; D010446:Peptide Fragments; D010450:Endopeptidases; D002918:Chymotrypsin