Abstract
The titration of ribonuclease, acid to its isoionic point, has been conducted in 1.80 M KCl. The slopes of the titration curves in the neighborhood of half neutralization of the carboxyl groups have been studied at several ionic strengths. It is concluded from these slopes that the influence of the electrical double layer around the protein ion on its titration behavior is negligible at and above an ionic strength of 0.15. The molar buffer capacities indicate a wide dispersion of the carboxyl intrinsic ionization constants. It is shown that the molar capacity of the carboxyl groups resemble more nearly those found for heat denatured bovine γ-globulin, bovine serum albumin, and egg albumin rather than the buffer capacities of the native forms of these proteins. The apparent intrinsic ionization constants of the carboxyl and imidazole groups have been estimated by graphical means.
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