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Isolation and Characterization of Angiotensin-Converting Enzyme Inhibitors from Agkistrodon halys halys Venom

Author:
L’vov, V. M., Sadykov, E. S., Yunusova, E. S., Shkinev, A. V.
Source:
Chemistry of natural compounds 2013 v.49 no.5 pp. 914-917
ISSN:
0009-3130
Subject:
Agkistrodon, enzyme inhibitors, peptidyl-dipeptidase A, venoms
Abstract:
The peptide fraction of venom from the Eastern pit viper Agkistrodon halys halys (Crotalidae) that was obtained by gel-filtration over Sephacryl S-100 HR exhibited high activity as an angiotensin-converting enzyme (ACE, EC 3.4.15.1) inhibitor. Separation of the materials over TSK HW-40F and SP-Sephadex C-25 produced purified (chromatographically pure) ACE inhibitors (ACEI) of molecular weight up to 2.5 kDa and IC₅₀values in the range 0.48–15.3 μg/mL.
Agid:
615687