Disc electrophoreses of human sera from 180 patients with various diseases were carried out, and the changes of electrophoretic patterns and the relative concentrations of the protein fractions were studied in comparison with those of 52 normal subjects reported in the previous paper (26).
1) In liver diseases, other than obstructive jaundice and cholecystitis, the number of protein fractions decreased and γ-globulin increased and showed two peaks in many cases. The haptoglobin bands were reduced in intensity especially in parenchymatous disorders of the liver. In obstructive jaundice and cholecystitis electrophoretic patterns were similar to those of normal subjects except that the haptoglobin zones appeared more clearly; prealbumin, albumin, α_L, α₁', α₂', F_α2, and β₂' decreased, and βγ, S_α2 and S_β increased. Transferrin decreased markedly in severe acute hepatitis, Banti's syndrome, Wilson's disease and hemochromatosis.
2) In renal diseases the characteristics of the electrophoretic patterns were that the haptoglobins appeared distinct and γ-globulin became decreased, whereas the number of protein fractions of sera from patients with renal diseases was not less than that of normal subject. Usually albumin decreased, and βγ, S_α2 and S_β increased. Transferrin and α_L increased markedly in nephrotic syndrome
3) In the patients with gastric cancer and peritonitis carcinomatosa three groups of sera could be distinguished: 1. Sera with electrophoretic patterns similar to those of normal, 2. sera with decreased haptoglobin bands, and 3. sera with increased haptoglobin bands. In leukemia the patterns showed many distinct haptoglobin bands and faint γ-globulin zone. Postalbumin (σ) was seen in many cases of malignant tumors, prealbumin and albumin decreased, βγ, S_α2 and S_β increased. Transferrin decreased markedly in sera from patients with gastric cancer and peritonitis carcinomatosa.
4) In inflammatory diseases, rheumatic fever, and rheumatic arthritis, haptoglobins increased.

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Specific absorption coefficients of electrophoretically separated human serum protein fractions were determined. Fresh normal sera from 5 healthy blood donors were pooled and submitted to starch grain zone electrophoresis using either phosphate buffer at pH8.0 or veronal buffer at pH8.6. Protein fractions were eluted with neutral saline and optical density at 280mμ and nitrogen contents were determined. Specific absorption coefficient, ε, at 280mμ was expressed as O. D. of the solution of each protein fraction at a concentration of 1mg protein nitrogen per ml measured in a 1cm cell.
Average values of ε for serum protein fractions obtained from six runs of electrophoresis with the phosphate buffer and six runs with the veronal buffer were as follows: albumin; 4.2, α-globulin; 6.7, β-globulin; 8.3, and γ-globulin; 9.5.
Results obtained by densitometric analysis at 280mμ of agar electrophoretic patterns of human sera were corrected for the above mentioned specific absorption coefficients by multiplying the optical densities of albumin, α-, β-, and γ-globulins by 16, 10, 8, and 7, respectively. Percentage value of each serum protein fraction thus obtained were found to be in good agreement with that obtained by free electrophoresis in 10 cases of normal and 6 cases of pathological sera.

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