Improved Method for High-performance Liquid Chromatography Assay of Angiotensin I Converting Enzyme Inhibitory Activity
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Abstract:
A modified method for determining the inhibitory activity of angiotensin-converting enzyme (ACE) from Pinctada martensi hydrolysate by HPLC was proposed. This method eliminated the effect of absorption peaks of some samples at the retention time of hippuric acid (HA) at 228 nm, and improved the measurement accuracy. The interfering peak area of the hydrolyzate decreased with increasing hydrolysis time. The interfering peak area of the hydrolysate by endogenous enzymes decreased to zero after 24 hours. The effects of different adding sequences of N-Hippuryl-His-Leu hydrate (HHL) and ACE on the assay were compared. Results showed that ACE inhibitory activity when HHL was added firstly was higher than those when ACE was added firstly. Therefore, in determination of ACE inhibitory activity, the same addition sequence of ACE and HHL should be adopted.
