VI. RELATIONSHIP BETWEEN ELECTRIC MOBILITY, CHARGE, AND TITRATION OF PROTEINS

Harold A. Abramson ¹

¹ From the Laboratory of General Physiology, Harvard University, Cambridge

1. By combining the theories of Smoluchowski, Debye and Hückel, and Henry it is possible to state explicitly (making necessary assumptions) under what conditions the following simple rule should be valid for proteins:

In solutions of the same ionic strength, the electric mobilities of the same protein at different hydrogen ion activities should be proportional to the number of hydrogen (hydroxyl) ions bound.

2. Data of Tiselius and of the writer confirm this rule for (a) egg albumin, (b) serum albumin, (c) deaminized gelatin and gelatin, and (d) casein.

3. On the basis of the confirmed theory the titration curves of certain proteins are predicted from their mobilities.

4. It is shown that when certain proteins are adsorbed by quartz the apparent dissociation constant of the adsorbed protein is practically unchanged. The mass law must also be valid at the phase boundary.

5. The facts of paragraphs (1) to (4) are discussed in connection with the mechanism of (a) protein adsorption, (b) enzyme activity, (c) immune reactions, (d) the calculation of the electric charge of cells, and (e) criteria of surface similarity.

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