An Assay for Angiotensin-Converting Enzyme Using Capillary Zone Electrophoresis

✍ Scribed by Rong-zhen Zhang; Xiao-hua Xu; Tian-bao Chen; Long Li; Ping-fan Rao

• Publisher: Elsevier Science
• Year: 2000
• Tongue: English
• Weight: 62 KB
• Volume: 280
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1006/abio.2000.4535

✦ Synopsis

A sensitive and rapid method was developed for angiotensin-converting enzyme (ACE) activity determination by capillary zone electrophoresis. Hippuryl-l-histidyl-l-leucine, a synthetic tripeptide, was used as the ACE-specific substrate. Capillary zone electrophoresis was employed to separate the products of the enzymatic reaction and the ACE activity was determined by quantification of hippuric acid, a result of the enzymatic reaction on the tripeptide. The capillary electrophoresis was performed in a 27 cm x 75 micrometer i.d. fused-silica capillary using 200 mM boric acid-borate buffer (pH 9.0) as a run buffer with an applied voltage of 8.1 kV at a capillary temperature of 23 degrees C. The electrophoresis was monitored at 228 nm. Each electrophoretic run requires only a nanoliter of the enzymatic reactant solution, at only 6 min, rendering a powerful tool for the ACE assay.