Abstract

The inhibiting effect of the proteins gelatine, albumine and histone on the polarographic reduction of several metal ions in acidic solutions has been discussed. It has been found that the differences in the double layer capacity at a mercury electrode in neutral and acidic solutions containing proteins cannot account for the substantial influence of pH on the inhibiting effect. It is suggested that the extremely low transfer coefficient for the inhibited cation reduction processes is due to the position of the energy barrier at a distance from the electrode comparable with the radius of a positively charged protein molecule.

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