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ARTICLE |
X. ELECTRIC MOBILITY AND CHARGE OF PROTEINS IN ALCOHOL-WATER MIXTURES
1. The electrophoretic velocities of gelatin-, egg-albumin-, and gliadin-covered quartz particles in various alcohol-water solutions are, within the limits employed in usual experimental procedures, proportional to the field strength.
2. The electrophoretic mobilities of small, irregularly shaped quartz particles covered with an adsorbed film of protein in alcohol-water solutions are equal to the electroosmotic mobilities of the liquid past similarly coated flat surfaces. Hence the size and shape of such particles does not influence their mobilities, which depend entirely on the protein film.
3. The corrected mobility and hence presumably the charge of gelatin-covered quartz particles in solutions containing 35 per cent ethyl alcohol is proportional to the combining power of the gelatin; therefore the gelatin is adsorbed with the active groups oriented toward the liquid. The same is true in 60 per cent alcohol.
4. The charge calculated by means of the Debye-Henry approximation from the mobility of gelatin in solutions containing up to 35 per cent ethyl alcohol is, in the neighborhood of the isoelectric point, proportional to the combining power of the gelatin. Therefore the dielectric constant and the viscosity of the bulk of the medium may be used in the Debye-Henry approximation
Q = 6 
r vm (1 + 
r)
to predict changes in charge from mobility.
5. In the neighborhood of the isoelectric point gelatin is probably completely ionized in buffered ethyl alcohol-water mixtures up to 60 per cent alcohol.
6. In the presence of ethyl alcohol the isoelectric point of gelatin is shifted toward smaller hydrogen ion activities. This shift, like that caused by alcohol in the isoelectric points of certain amino acids, is approximately linearly related to the dielectric constant of the medium.
Accepted on October 10, 1932
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