The initial objective of this investigation was the measurement of the isoelectric pH values of ß-lactoglobulin as a function of the ionic strength of the buffer solvent and the nature of added salt ions. In contrast to their experience with egg albumin, Cannan, Palmer, and Kibrick (4) found that the pH of a ß-lactoglobulin solution is independent of the concentration of added potassium chloride and is identical with the isoelectric pH value obtained by Pedersen ( 14). On the basis of these observations they suggested that the isoelectric pH values of this protein might prove to be independent of the ionic strength. Consequently we were somewhat surprised to find that the isoelectric pH of ß-lactoglobulin changed with the concentration of the acetate buffers in much the same manner that Tiselius and Svensson (21) had observed in the case of egg albumin.We then studied bovine serum albumin and found that this protein behaves similarly to egg albumin and ß-lactoglobulin. Finally, in an attempt to learn 1 Presented at the Twenty-second National Colloid Symposium, which was held under the auspices of the Division of Colloid Chemistry of the American Chemical Society at
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