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Presence and comparison of angiotensin converting enzyme in commercial cell culture sera
Author(s) -
Bramucci Massimo,
Miano Antonino,
Quassinti Luana,
Maccari Ennio,
Murri Oretta,
Amici Domenico
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900201103
Subject(s) - bradykinin , lisinopril , enzyme , pentapeptide repeat , captopril , in vitro , angiotensin converting enzyme , cell culture , biochemistry , renin–angiotensin system , enzyme assay , chemistry , microbiology and biotechnology , biology , peptide , endocrinology , receptor , genetics , blood pressure
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°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”.