Journal of Dairy Science · 1963 · 321 citations · 16 references
Life SciencesBiochemistryMolecular BiologyStructural BiochemistryStructural BiologyAffinity ChromatographyCasein ChemistryEnzyme PurificationMilk ProteinsProtein PurificationProtein StructureCasein Fractionation
Summary α s -Casein and κ -casein have been freed of major contaminants, judged by starch-gel-urea electrophoresis. The α s -casein was prepared by a urea-sodium chloride procedure with a final precipitation of impurities by ethanol. κ -Casein was prepared by extraction of whole casein with urea-sulfuric acid supplemented with ethanol precipitation. Electrophoretic mobility, pH of minimal solubility salt-free (isoionic point), and with 0.1 m NaCl (isoelectric point), ultraviolet absorption, and interaction with calcium ions are reported.
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Buffers of pH 2 to 12 for use in electrophoresis.