Published: Journal of Chromatographic Science, Volume 34, Number 8, August 1996, pp. 358–361.
A Modified Procedure for
Caseinophosphopeptide Analysis
J.-H. Lin and B.-H. Chiang
A modified procedure is established for analyzing caseinophosphopeptides. The sodium caseinate hydrolysate is first treated by immobilized metal ion affinity chromatography to enrich the phosphopeptides. Because of the formation of Fe3+–peptide complexes, ethylenediaminetetraacetic acid is added to the bound fraction eluted with the immobilized metal ion affinity chromatography to disintegrate the complexes. Thus, the subsequent high-performance liquid chromatographic analysis is facilitated. A stepwise gradient elution is also suggested to enhance the resolution of caseinophosphopeptides during high-performance liquid chromatographic analysis.
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