A modified procedure for caseinophosphopeptide analysis.
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 Fe(3+)-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.
Lin
J H
JH
Graduate Institute of Food Science and Technology, National Taiwan University, Taipei, Republic of China.
Chiang
B H
BH
D000595:Amino Acid Sequence; D002364:Caseins / Q000032:analysis*; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004492:Edetic Acid; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000032:analysis*; D011492:Protein Hydrolysates / Q000032:analysis*; D014357:Trypsin
D002364:Caseins; D010748:Phosphopeptides; D011492:Protein Hydrolysates; D004492:Edetic Acid; D014357:Trypsin