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- W2004286554 abstract "Paper-electrophoretic separation of intrinsic factor-related “primary” and “secondary” B12 binders in pooled normal human gastric juice was achieved by using Teorell-Stenhagen buffers of pH 4.0–5.0, at which pH the “primary” binder moves to the cathode, while the “secondary” one travels to the anode. The isoelectric point of the “primary” binder is about pH 5.5, while that of the “secondary” one is pH 2.5–3.0. The electrophoretic mobility of none of the major carbohydrate-, proteinor peptide-nondialyzable components of gastric juice correlates with that of the “primary” or “secondary” B12 binders when run on electrophoresis in the pH range of from 2.5 to 10.0. This supports previous conclusions that none of the major components of gastric juice resolved by paper electrophoresis represents the intrinsic factor-related B12 binders." @default.
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- W2004286554 date "1964-05-01" @default.
- W2004286554 modified "2023-10-16" @default.
- W2004286554 title "Separation of “primary” and “secondary” B12 binders in human gastric juice by paper electrophoresis at low pH" @default.
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- W2004286554 doi "https://doi.org/10.1016/0009-8981(64)90086-5" @default.
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