Electrophoretic mobilities of bovine serum albumin (SA), haemoglobin (
Hb) and ovalbumin (OA) have been determined by direct ultramicroscopic
observation of the velocities of individual particles in a particle e
lectrophoresis apparatus, and of SA and Hb in a free-flow apparatus of
the type described independently by Hannig and by Strickler. Agreemen
t between the results obtained by the two methods for SA and Hb over w
ide pH ranges covering both sides of the respective isoelectric points
was surprisingly good. Runs were also conducted in the free-flow cell
in which SA was transported in buffer containing Hb, and vice versa;
these showed clear evidence of interactions between the motions of the
two proteins, as occurs in the parallel case of multicomponent diffus
ion, but the results could not be quantified in terms of the Maxwell-S
tefan theory. Finally, the single protein data were compared with pred
ictions made on the basis of the Debye-Huckel-Henry theory, and showed
reasonable agreement.