A rapid, simple, and accurate method for the chemical assay of angiotensin-converting enzyme has been developed. The method relies on previously published method for spectrophotometric assay of angiotensinconverting enzyme activity and on the use of 2,4,6-trichloro-s-triazine (TT) as a calorimetric
A continuous spectrophotometric assay for angiotensin converting enzyme
✍ Scribed by Barton Holmquist; Peter Bünning; James F. Riordan
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 701 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Furanacryloyl tripeptides conforming to the known substrate specificity of the angiotensin converting enzyme (dipeptidyl carboxypeptidase, EC 3.4.15.1) have been employed to provide a continuous spectrophotometric assay for this peptidase in the visible region. The assay is based on a blue shift of the absorption spectrum that occurs upon hydrolysis of the substrate to produce a furanacryloyl-blocked amino acid and a dipeptide. Of the various furanacryloyl tripeptides tested, furanacryloyl+phenylalanylglycylglycine exhibits the most suitable characteristics for routine assays of angiotensin converting enzyme.
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