Partial Purification of Angiotensin Converting Enzyme Inhibitory Peptide Isolated form Supernatant of Bovine Plasma Treated by Trichloroscetic Acid

  • Park, Eun-Hee (Dept. of Food Science and Technology , Chungnam National University) ;
  • Song, Kyung-Bin (Dept. of Food Science and Technology , Chungnam National University)
  • Published : 1998.12.01

Abstract

An angiotensin converting enzyme (ACE) inhibitor was isolated and partially purified from bovine blood plasma. Bovine blood plasma was obtained after removing blood cells by centrifugation, followed by the addition of anticoagulant to whole bovine blood. To precipitate plasma proteins, bovine blood plasma was treated with 4% trichloroacetic acid (TCA) as a final concentration .An ACE inhibitor was isolated from TCA supernatnat, using ultrafiltration, gel permeation chormatography, and reverse-phase high pressure liquid chromatogrpahy. The ACE inhibitor purified from TCA supernatant had IC50 values of 9.4$\mu$M.