Amino acid sequence of penicillopepsin. III. Isolation and characterization of amino terminal, tryptic, and tryptophanyl peptides.
The amino acid sequence 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.
D000595:Amino Acid Sequence; D010450:Endopeptidases; D010406:Penicillins; D010407:Penicillium / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D013381:Subtilisins; D014357:Trypsin; D014364:Tryptophan / Q000032:analysis
D010406:Penicillins; D010446:Peptide Fragments; D014364:Tryptophan; D010450:Endopeptidases; D013381:Subtilisins; D014357:Trypsin