Anti-Free-Radical Properties of the Peptide Fractions Isolated from String Bean by Immobilized Metal Ion Affinity Chromatography
In this study, peptides and proteins extracted from string bean with 1% TCA were separated by chromatography on columns with copper ions immobilized through IDA and o-phosphoserine OPS. Protein and peptide concentrations and the anti-free-radical properties of the isolated fractions were determined. Identification was obtained using mass spectrometry. The anti-free- radical activity of all analyzed samples was determined using the DPPH· test, and was found to depend on reaction time, choice of chelating agent and the order in which the fractions were eluted from the column.
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Document Type: Research Article
Publication date: 2007-05-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.