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handle: 10261/55330
The purification of a peptidic fraction with angiotensin converting enzyme (ACE) inhibitory activity from sunflower protein hydrolysates by affinity chromatography was recently described. We now describe that reverse-phase HPLC fractionation of this product yields several fractions with IC50 one order of magnitude higher than those previously purified by reverse-phase HPLC following gel filtration chromatography, showing that affinity chromatography is much more effective than gel filtration chromatography as a first step for purification of ACE inhibitory peptides. The amino acid composition of these fractions is presented, but attempts to determine their amino acid sequence failed, showing that these fractions contained more than one peptide.
This work was supported by research grants AGL 2004-03930 (F.M.) and AGL 2005-01120 (J.G.-C.) from the Spanish Ministry of Education and Science, partially supported by FEDER funds from EU.
Peer reviewed
Inhibitory peptides, Affinity purification, Angiotensin converting enzyme, Sunflower protein hydrolysate
Inhibitory peptides, Affinity purification, Angiotensin converting enzyme, Sunflower protein hydrolysate
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