Abstract
Levels of angiotensin converting enzyme (ACE) in cultured bovine pulmonary artery endothelial cells treated with dexamethasone, aldosterone, 3,3′,5′-triiodo-L-thyronine, Ca 2+ ionophore, 3-isobutyl-1-methylxanthine, dibutyry1 cAMP and forskolin were quantitated by an enzyme linked immunosorbent assay (ELISA). The configuration for the ELISA consisted of purified bovine lung ACE adsorbed to a solid phase competing with endothelial cellullar ACE for a limited amount of anti-ACE immunoglobulin. ACE-IgG complex on the solid phase was detected by goat anti-rabbit IgG-alkaline phosphatase conjugate with enzymatic activity measured by p-nitrophenylphosphate as substrate. This ELISA detected ACE with a sensitivity of 32 ng/ml cellular ACE. Elevation in cellular ACE catalytic activity as measured by fluorescent assay of detergent extracts from bovine endothelial cells corresponded well with an increase in ACE protein as determined by the ELISA. These results provide direct evidence that increases in catalytic activity of ACE produced in endothelial cells by a variety of agents result from enhancement of the synthesis of ACE protein.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
