Isolation of angiotensin-converting enzyme inhibitor from tuna muscle

A novel inhibitor of angiotensin-converting enzyme (ACE) has been discovered and isolated in a pure form from acid extract of tuna muscle by successive column chromatographies and HPLC. The final preparation showed IC 50 values of 1 μM and 2 μM for ACEs from bovine and rabbit lungs, respectively. Th...

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Veröffentlicht in:	Biochemical and biophysical research communications 1988-08, Vol.155 (1), p.332-337
Hauptverfasser:	Kohama, Yasuhiro, Matsumoto, Shigeru, Oka, Hiroaki, Teramoto, Tetsuyuki, Okabe, Masaru, Mimura, Tsutomu
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals Biological and medical sciences Cattle chromatographic techniques Chromatography, Gel Chromatography, High Pressure Liquid dipeptidyl carboxypeptidase I enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases inhibitors Marine Molecular Sequence Data Molecular Weight muscles Muscles - analysis Neothunnus macropterus Oligopeptides - isolation & purification Rabbits Tuna ultrastructure
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Beschreibung
Zusammenfassung:	A novel inhibitor of angiotensin-converting enzyme (ACE) has been discovered and isolated in a pure form from acid extract of tuna muscle by successive column chromatographies and HPLC. The final preparation showed IC 50 values of 1 μM and 2 μM for ACEs from bovine and rabbit lungs, respectively. The amino acid sequence of the inhibitor has been established as Pro-Thr-His-Ile-Lys-Trp-Gly-Asp by the Edman procedure and carboxypeptidase digestion.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/S0006-291X(88)81089-1