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- W2128996934 abstract "Summary Tryptic phosphopeptides were obtained from whole bovine casein by chromatography on the anion exchange resin QAE-Sephadex A 25. Salt gradient elution of the column allowed separation of non-phosphorylated peptides from phosphorylated species. The preparations obtained contained at least seven distinct phosphopeptides of which the following casein fragments were identified: α s1 (43–58):2P, α s1 (59–79): 5P, α s2 (46–70): 4P, β(1–28): 4P, β(2–28): 4P, and β(33–48): 1P. Fast protein liquid chromatography (FPLC) on Mono Q HR 5/5 resin showed that the phosphopeptides were eluted in the same order as from the QAE-Sephadex resin. However, on the analytical column HR 5/5 the fragments α s1 (59–79): 5P and β(2–28): 4P, having the same net charge under the conditions of chromatography, co-eluted, whereas they were at least partly separated on the preparative column HR 16/10. Following enzymic dephosphorylation, the peptides eluted at lower salt strength in the gradient. FPLC on Mono Q resin thus permitted dephosphorylation to be monitored and intermediates between the parent species and the fully dephosphorylated peptide to be identified." @default.
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- W2128996934 date "1989-08-01" @default.
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- W2128996934 title "Tryptic phosphopeptides from whole casein. I. Preparation and analysis by fast protein liquid chromatography" @default.
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- W2128996934 doi "https://doi.org/10.1017/s0022029900029125" @default.
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