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Binding of Copper by Certain Milk Proteins as Measured by Equilibrium Dialysis¹

Department of Food Science and Human Nutrition, Michigan State University, East Lansing 48823

ABSTRACT

The binding of copper with micellar casein, fat globule-membrane protein (soluble fraction), -casein (crude), ß-casein and ß-lactoglobulin was determined by equilibrium dialysis at pH 6.5. Solutions of these proteins at 200.0, 300.0, 243.6, 120.5 and 142.0 mg/liter were placed in washed bags and dialyzed against each of four copper solutions for 72 hours, an interval sufficient to attain equilibrium. Four copper solutions outside the dialysis bags were 16 x 10^-6, 32 x 10^-6, 64 x 10^-6 or 80 x 10^-6 M. Data were plotted in moles of bound copper per mole of protein against the logarithm of concentration of unbound copper. Micellar casein bound the most copper. The fat-globule membrane protein had the second greatest affinity for copper ions. Much less copper was bound by -casein, ß-lactoglobulin and ß-casein.

¹ Published with the approval of the Director of the Michigan Agricultural Experiment Station as Journal Article 4778.

² Present address: Meyer-Blanke Company, 5432 Highland Park Drive, St. Louis, Missouri.