A method is described for the selective purification of 32P-labeled peptides for sequence analysis. The procedure is based on the differential retention on reversed-phase high-performance liquid chromatography of the peptide containing phosphoserine versus dehydroalanine obtained by alkaline β-elimination of the phosphate. The method was tested using two synthetic phosphopeptides representing the phosphorylation site in pyruvate kinase and one of the sites in glycogen synthase.
ASJC Scopus subject areas
- Analytical Chemistry