Effect of Temperature on Composition of Casein Fractions Eluted from Diethylaminoethyl Cellulose Column

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Abstract
The chromatographic behavior of isoelectric casein on DEAE cellulose column at room temperature and in cold was compared. The casein was eluted from the column with the stepwise increase of NaCl concentration in phosphate buffer of pH 7. The caseins were less tightly adsorbed to the adsorbent and eluted at lower concentration of NaCl at 4[degree]C than at 25[degree]. The composition of the eluted casein fractions was examined by urea starch gel electro-phoresis with addition of 2-mercaptoethanoL Although none of the casein fractions were homogeneous, [beta]-casein entirely free from [alpha]sl-and K-caseins can be prepared without urea by the DEAE chromatography at AX. At 25[degree]C the major portions of K-casein were eluted with 0-casein, but at 4t they were eluted in between the major fractions of [beta]-casein and [alpha]s-casein.

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