A colorimetric method and a capillary electrophoresis procedure were developed for quantifying histidyl-leucine and hippurate, respectively. The colorimetric method is sensitive (extinction coefficient = 7.5 mM(-1) cm(-1)) and reproducible (CV = 1.7%, n = 5), which is based on a selective chromogeni
A fluorogenic substrate for angiotensin-converting enzyme
β Scribed by Anders Persson; Irwin B. Wilson
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 406 KB
- Volume
- 83
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A fluorogenic substrate for the angiotensin-converting enzyme (EC 3.4.15.1) is presented: para-nitrobenzyloxycarbonylglycyl-~-tryptophylglycine.
The assay is based upon relief of the internal quenching of tryptophan fluorescence by the nitrobenzyl group when the substrate is enzymatically hydrolyzed to produce para-nitrobenzyloxycarbonylglycine and tryptophylglycine. The new substrate has a K, of 9 x 10e4 M at 37Β°C and pH 7.4 and is rapidly hydrolyzed in comparison with other substrates. We also describe the use of fluorescamine to assay the dipeptides released from N-blocked substrates by the converting enzyme.
π SIMILAR VOLUMES
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 prod