Potentiometric analysis of pure animal proteins

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Abstract
[long dash]The iso-electric points of egg-albumin, serum-albumin, Hb and caseinogen, det''d. by the potentiometric measurement of the pH of each protein after purification by dialysis and electrodialysis controlled by conductivity measurements, were, respectively, pH 4.7-4.85; 5.4-5.5; 6.5-6.6; and 5.6-5.8. Stoichiometric relationships of the combination of proteins with acids and bases were studied. The no. of gram-equivalents of each, required to fix 1 gm.-equivalent of OH", were, respectively, 3420, 5450, 6800, and 860; to fix 1 gm-equiv. of H+, 18000, 12900, 9200, and 5000. The dissociation constants of the proteins, as acid (Ka) were, respectively, 3.6 X 10-7, 5.5 X 10-8, 1.2 X 10-8, and 5.0 X10-8; as bases (Kb), respectively, 2.8-10-11, 2.7 X 10-10, 7.6 X 10-10, and 3.0 X 10-10. Mol. wts. were, respectively, 34,500, 67,500, 68,000, and 98,000; No. of COOH groups capable of dissociation, 10, 12.3, 10, and 114; and no. of NH2 groups capable of dissociation, 1.9, 5.2, 7.4, and 19.6.

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