title: Inhibition and inhibition kinetics of angiotensin converting enzyme activity by hemorphins, isolated from a peptic bovine hemoglobin hydrolysate.
abstract: The inhibitory effect on angiotensin converting enzyme (ACE) activity by hemorphins isolated from an enzymatic bovine hemoglobin hydrolysate was reported. Inhibitory kinetics proved that inhibition mechanism was non-competitive. The stability of hemorphins towards ACE was studied.
authors.affiliation: Laboratoire de Génie Protéique, Université de La Rochelle, France.
authors.forename: Q
authors.initials: Q
authors.lastname: Zhao
authors.forename: F
authors.initials: F
authors.lastname: Sannier
authors.forename: I
authors.initials: I
authors.lastname: Garreau
authors.forename: D
authors.initials: D
authors.lastname: Guillochon
authors.forename: J M
authors.initials: JM
authors.lastname: Piot
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D006454:Hemoglobins / Q000737:chemistry* / Q000494:pharmacology; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D006454:Hemoglobins; D010446:Peptide Fragments; D007703:Peptidyl-Dipeptidase A