Isolation of angiotensin-converting enzyme inhibitor from tuna muscle

Biochem Biophys Res Commun. 1988 Aug 30;155(1):332-7. doi: 10.1016/s0006-291x(88)81089-1.

Abstract

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 IC50 values of 1 microM and 2 microM 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.

MeSH terms

  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
  • Animals
  • Cattle
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Molecular Sequence Data
  • Molecular Weight
  • Muscles / analysis*
  • Oligopeptides / isolation & purification
  • Rabbits
  • Tuna

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Oligopeptides
  • tuna AI