Abstract
An experimental study has been made of the adsorption of purified egg albumin, from aqueous solution, on collodion membranes. At protein concentrations of 4 to 7 per cent apparent saturation values were obtained which resembled closely the results obtained with gelatin, showing a maximum at pH 5.0 and lower values on either side of this region. Over large ranges of protein concentration, however, the curves for the adsorption from solutions removed in either direction from the isoelectric point exhibited a different shape from the hyperbola obtained in the neighborhood of pH 5.0. The addition of NaCl to solutions on the acid side tended to obliterate the effect of the pH difference; on the alkaline side it greatly increased the adsorption. The adsorption at 25 degrees was about twice as great as that at 1 degrees . The theory of the swelling of submicroscopic particles, advanced to account for the adsorption behavior of gelatin, is not sufficient to explain the results obtained with egg albumin. It is suggested that the effect is related to alterations in the forces causing the retention of the protein on the membranes.