title: The degradation of bioactive peptides and proteins by dipeptidyl peptidase IV from human placenta.
abstract: The degradation of several bioactive peptides and proteins by purified human dipeptidyl peptidase IV is reported. It was hitherto unknown that human gastrin-releasing peptide, human chorionic gonadotropin, human pancreatic polypeptide, sheep prolactin, aprotinin, corticotropin-like intermediate lobe peptide and (Tyr-)melanostatin are substrates of this peptidase. Kinetic constants were determined for the degradation of a number of other natural peptides, including substance P, the degradation of which has been described earlier in a qualitative manner. Generally, small peptides are degraded much more rapidly than proteins. However, the Km-values seem to be independent of the peptide chain length. The influence of the action of dipeptidyl peptidase IV on the biological function of peptides and proteins is discussed.
authors.affiliation: Arbeitsgruppe Gesundheitswissenschaften, Universität, Osnabrück.
authors.forename: I
authors.initials: I
authors.lastname: Nausch
authors.forename: R
authors.initials: R
authors.lastname: Mentlein
authors.forename: E
authors.initials: E
authors.lastname: Heymann
mesh_terms: D000595:Amino Acid Sequence; D018819:Dipeptidyl Peptidase 4; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D010920:Placenta / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D018819:Dipeptidyl Peptidase 4