Presence and comparison of angiotensin converting enzyme in commercial cell culture sera

Biochem Mol Biol Int. 1999 Jan;47(1):107-15. doi: 10.1080/15216549900201103.


This study was conducted to determine the presence of the angiotensin converting enzyme in commercial sera used in cell culture medium. The aim of the research was to bring the presence of proteinases (angiotensin converting enzyme) to cell culture users' knowledge and to give some data for solving problems about the development of peptides as useful drugs. The enzymes, purified from foetal bovine, adult bovine, foetal equine, adult equine, and human sera, showed molecular weights of about 170 kDa. Captopril and lisinopril inhibited enzyme activities at nanomolar concentrations. The enzymes were able to hydrolyze, with different efficiency, angiotensin I, bradykinin and epidermal mitosis inhibiting pentapeptide. The heat inactivation of commercial sera at 56 degrees C for 30 min showed a reduction of ACE activity of about 35-80%. Therefore, the presence of ACE activity in commercial sera can influence the activity of biological peptides tested on cell lines cultured "in vitro."

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin II / metabolism
  • Animals
  • Blood Proteins / metabolism
  • Bradykinin / metabolism
  • Captopril / metabolism
  • Cattle
  • Culture Media / chemistry*
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases / analysis*
  • Horses / blood
  • Humans
  • Inhibitory Concentration 50
  • Kinetics
  • Lisinopril / metabolism
  • Oligopeptides / metabolism
  • Peptidyl-Dipeptidase A / analysis*
  • Silver Staining


  • Blood Proteins
  • Culture Media
  • Oligopeptides
  • Angiotensin II
  • 2-furanacryloyl-phenylalanyl-glycyl-glycine
  • Captopril
  • Lisinopril
  • Endopeptidases
  • Peptidyl-Dipeptidase A
  • Bradykinin