The study of substrate specificity of a new peptide substrate of endothelin-converting enzyme

A new hexapeptide CMC-Ala-Gly-Gly-Trp-Phe-Arg was used as a substrate for assay of endothelin-converting (ECE; EC 3.4.24.71) and angiotensin-converting (ACE; EC 3.4.15.1) enzymes and of neutral endopeptidase (NEP; EC 3.4.24.11). The specific inhibitors lisinopril (for ACE) and thiorphan (for NEP) we...

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Bibliographic Details
Published in:Biochemistry (Moscow). Supplement. Series B, Biomedical chemistry Biomedical chemistry, 2007-09, Vol.1 (3), p.210-215
Main Authors: Gureeva, T. A., Kugaevskaya, E. V., Pozdnev, V. F., Prozorovskii, V. N., Eliseeva, Yu. E., Solovyeva, N. I.
Format: Article
Language:English
Subjects:
Bioassays
Biochemistry
Enzymes
Peptides
Substrates
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Summary:A new hexapeptide CMC-Ala-Gly-Gly-Trp-Phe-Arg was used as a substrate for assay of endothelin-converting (ECE; EC 3.4.24.71) and angiotensin-converting (ACE; EC 3.4.15.1) enzymes and of neutral endopeptidase (NEP; EC 3.4.24.11). The specific inhibitors lisinopril (for ACE) and thiorphan (for NEP) were used for discrimination between activities of these enzymes.[PUBLICATION ABSTRACT]
ISSN:1990-7508
1990-7516
DOI:10.1134/S1990750807030055