title: Carboxypeptidase inhibitors from Ascaris suum: the primary structure.
abstract: The carboxypeptidase A inhibitor from Ascaris suum was isolated from aqueous extracts by affinity chromatography toward immobilized carboxypeptidase A. The amino acid sequence is DQVRKCLSDT10DCTNGEKCVQ20KNKICSTIVE30IQRCEKEHFT40IPCKSNNDCQ50VWAHEKICN K60LPWGL65 . The carboxypeptidase A inhibitor is not homologous with the chymotrypsin/elastase or trypsin inhibitors from Ascaris, but shows homology in a 9-residue internal sequence with the 37/39-residue carboxypeptidase inhibitors from tomato and potato. The carboxy-terminal 5 (4) residues in the three inhibitors are similar, suggesting a common mechanism of inhibition.
authors.affiliation: Department of Biochemistry, Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612.
authors.forename: G A
authors.initials: GA
authors.lastname: Homandberg
authors.forename: R D
authors.initials: RD
authors.lastname: Litwiller
authors.forename: R J
authors.initials: RJ
authors.lastname: Peanasky
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D001200:Ascaris / Q000378:metabolism*; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D043422:Carboxypeptidases A; D002846:Chromatography, Affinity; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D004800:Enzymes, Immobilized; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D012689:Sequence Homology, Nucleic Acid; D011198:Solanum tuberosum / Q000201:enzymology; D014357:Trypsin
chemical_list: D000596:Amino Acids; D004791:Enzyme Inhibitors; D004800:Enzymes, Immobilized; D010446:Peptide Fragments; D002268:Carboxypeptidases; D010447:Peptide Hydrolases; D043422:Carboxypeptidases A; D014357:Trypsin