Inhibition and inhibition kinetics of angiotensin converting enzyme activity by hemorphins, isolated from a peptic bovine hemoglobin hydrolysate.
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.
Zhao
Q
Q
Laboratoire de Génie Protéique, Université de La Rochelle, France.
Sannier
F
F
Garreau
I
I
Guillochon
D
D
Piot
J M
JM
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
D000806:Angiotensin-Converting Enzyme Inhibitors; D006454:Hemoglobins; D010446:Peptide Fragments; D007703:Peptidyl-Dipeptidase A