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Inhibition of angiotensin converting enzyme activity by five Senecio species.

Authors :
Loizzo, M.R.
Tundis, R.
Conforti, F.
Statti, G.A.
Menichini, Federica
Source :
Pharmaceutical Biology. Jun2009, Vol. 47 Issue 6, p516-520. 5p. 2 Charts, 1 Graph.
Publication Year :
2009

Abstract

In our continuous search of biological properties of Senecio species (Compositae), we investigated S. ambiguus subsp. ambiguus (Biv.) DC , S. gibbosus subsp. gibbosus DC , S. leucanthemifolius Poiret , S. inaequidens DC , and S. vulgaris L. for their angiotensin converting enzyme (ACE) inhibitory activity through an in vitro bioassay based on the enzymatic cleavage of the chromophore-fluorophore labelled substrate dansyltriglycine into dansylglycine, which is quantitatively measured by HPLC. Among analyzed extracts, ethyl acetate demonstrated the highest activity with IC50 values of 192.1 and 219.1 μg/mL for S. ambiguus subsp. ambiguus and S. inaequidens, respectively. Flavonoids were detected in these extracts on TLC sprayed with Natural Products reagent - polyethylene glycal reagent (NP/PEG). [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
13880209
Volume :
47
Issue :
6
Database :
Academic Search Index
Journal :
Pharmaceutical Biology
Publication Type :
Academic Journal
Accession number :
43539283
Full Text :
https://doi.org/10.1080/13880200902845787