An assay for angiotensin-converting enzyme using capillary zone electrophoresis |
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Authors: | Zhang R Xu X Chen T Li L Rao P |
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Institution: | Institute of Biotechnology, Fuzhou University, Fujian, 350002, People's Republic of China. |
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Abstract: | 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. |
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Keywords: | angiotensin-converting enzyme hippuryl-sciencedirect
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-leucine hippuric acid capillary electrophoresis |
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