Abstract
AbstractThe dielectric dispersion of ovalbumin solution was studied in the presence of various ions. It was found that ions such as tetraethylammonium, ammonium, Na, and K which are not bound to the protein had no effect on the dielectric increment or on the relaxation time. On the contrary, the addition of ions such as Cu, Ca, Mg, and H ions had a considerable effect on the dielectric increment as well as on the binding of the ions to the protein. These results indicate that ions do not affect the dielectric dispersion parameters of this protein unless they have specific interaction with the polar sites of the ovalbumin molecule. The electric polarization of protein solutions is discussed and it is suggested that the ion fluctuation process including the Maxwell‐Wagner effect is not necessarily the essential mechanism of dielectric polarization of isoelectric protein solutions.
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