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.
Publication types
-
Comparative Study
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Amino Acids / isolation & purification
-
Animals
-
Ascaris / metabolism*
-
Carboxypeptidases / antagonists & inhibitors*
-
Carboxypeptidases A
-
Chromatography, Affinity
-
Enzyme Inhibitors / isolation & purification*
-
Enzymes, Immobilized
-
Molecular Sequence Data
-
Molecular Weight
-
Peptide Fragments / analysis
-
Peptide Hydrolases
-
Sequence Homology, Nucleic Acid
-
Solanum tuberosum / enzymology
-
Trypsin
Substances
-
Amino Acids
-
Enzyme Inhibitors
-
Enzymes, Immobilized
-
Peptide Fragments
-
Carboxypeptidases
-
Peptide Hydrolases
-
Carboxypeptidases A
-
Trypsin