Purification and assay methods for angiotensin-converting enzyme.

Abstract

Angiotensin-converting enzyme (ACE; EN 3.4.15.1) is a peptidyl dipeptide hydrolase that removes the carboxyl terminal His-Leu from angiotensin I to produce the octapeptide angiotensin II. In addition, ACE inactivates bradykinin, a vasodilator peptide/mediator of inflammation, as well as substance P, enkephalins and endorphins. Because of the importance of ACE and its active site-directed inhibitors in the pathogenesis and treatment of cardiovascular disorders such as hypertension and heart failure, ACE purification and assay are of clinical and commercial, as well as scientific interest. This review summarizes the historical development of ACE purification and assay methods and presents some innovative high-performance liquid chromatography-based techniques developed in our own laboratory for high yield and efficient purification and sensitive and specific assay of ACE.

• Authors: Q C Meng, S Oparil
• Journal: Journal of chromatography. A (J Chromatogr A) Vol. 743 Issue 1 Pg. 105-22 (Aug 30 1996) ISSN: 0021-9673 [Print] Netherlands
• PMID: 8817875 (Publication Type: Journal Article, Review)

Chemical References

• Enzymes, Immobilized
• Renin

Topics

• Animals
• Blotting, Western
• Chromatography, Affinity
• Chromatography, High Pressure Liquid
• Electrophoresis, Polyacrylamide Gel
• Enzymes, Immobilized (chemistry)
• Humans
• Kidney (enzymology)
• Lung (enzymology)
• Male
• Prostate (enzymology)
• Radioimmunoassay
• Renin (isolation & purification, metabolism)
• Semen (enzymology)