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.

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Bibliographische Detailangaben
Veröffentlicht in:	Biochemical and biophysical research communications 1994-10, Vol.204 (1), p.216-223
Hauptverfasser:	Zhao, Q.Y., Sannier, F., Garreau, I., Guillochon, D., Piot, J.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Angiotensin-Converting Enzyme Inhibitors - pharmacology Animals Cattle Chromatography, Gel Hemoglobins - chemistry Hemoglobins - pharmacology Hydrolysis Kinetics Molecular Sequence Data Peptide Fragments - isolation & purification Peptide Fragments - metabolism Peptide Fragments - pharmacology Peptidyl-Dipeptidase A - metabolism Substrate Specificity
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Beschreibung
Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1994.2447