THE COMBINATION OF SALTS AND PROTEINS. I

Abstract

1. It has been found that the ratios of the total concentrations of Ca, Mg, K, Zn, inside and outside of gelatin particles do not agree with the ratios calculated according to Donnan's theory from the hydrogen ion activity ratios. 2. E.M.F. measurements of Zn and Cl electrode potentials in such a system show, however, that the ion activity ratios are correct, so that the discrepancy must be due to a decrease in the ion concentration by the formation of complex ions with the protein. 3. This has been confirmed in the case of Zn by Zn potential measurements in ZnCl2 solutions containing gelatin. It has been found that in 10 per cent gelatin containing 0.01 M ZnCl2 about 60 per cent of the Zn++ is combined with the gelatin. 4. If the activity ratios are correctly expressed by Donnan's equation, then the amount of any ion combined with a protein can be determined without E.M.F. measurements by determining its distribution in a proper system. If the activity ratio of the hydrogen ion and the activity of the other ion in the aqueous solution are known, then the activity and hence the concentration of the ion in the protein solution can be calculated. The difference between this and the total molar concentration of the ion in the protein represents the amount combined with the protein. 5. It has been shown that in the case of Zn the values obtained in this way agree quite closely with those determined by direct E.M.F. measurements. 6. The combination with Zn is rapidly and completely reversible and hence is probably not a surface effect. 7. Since the protein combines more with Zn than with Cl, the addition of ZnCl2 to isoelectric gelatin should give rise to an unequal ion distribution and hence to an increase in swelling, osmotic pressure, and viscosity. This has been found to be the case.