Amino acid sequence of penicillopepsin. III. Isolation and characterization of amino terminal, tryptic, and tryptophanyl peptides

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Abstract
The amino acid sequences of peptides isolated from a tryptic digest of penicillopepsin (EC 3.4.23.7), a subtilisin (EC 3.4.21.14) digest of maleylated penicillopepsin, and a chymotryptic digest of penicillopepsin modified with dinitrophenylsulfenyl (DNPS) chloride have been determined. The first two digests identified four of the five lysyl residues of the enzyme as well as the N-terminal peptide. The third digest provided overlaps at three of the tryptophanyl residues. The DNPS-tryptophan peptides were isolated on an affinity column prepared by coupling dinitrophenyl antibody raised in sheep to cyanogen bromide-activated Sepharose.