strength) was slightly lower than that obtained from the experi-
ments with collodion, extrapolating to pH 4.845 at p 0 (seeFig. 2).
Examination of acetate buffers containing 1 per cent of ovalbu-
min gave apparent isoelectric points which again determined a
straight line when plotted against the ionic strength (p 0.025,
0.050, and 0.100). The pH value of the isoelectric point for each
concentration of the buffer was distinctly lower than that at the
corresponding ionic strength with 0.1 per cent protein present; the
E. R. B. Smith 191
intercept with 0 ionic strength was at pH 4.825 (see Fig. 2). This
suggests that the protein has an amphoionic strength which tends
to lower its own apparent isoelectric point as does the increasing
of buffer concentration.
4.85’
q4.75 *
a
0.5 10 1.5 2.0
Alb umiQ ConceQtratio~ ip per cent,
FIQ. 4. The isoelectric points of ovalbumin at different concentrations
in buffers at 0 ionic strength plotted against the concentration of the
protein. 0 represents values from mobility measurements; 0 from mini-
mal pH change.