I carried out the electrophoretic analyses of serum protein of pulmonary tuberculosis, and studied about the following subjects.
1. Serum protein and the classification of pulmonary tuberculosis.
2. Serum protein and the blood cell sedimentation rate.
3. The variation of serum protein of tuberculous patients treated with chemotherapy and surgical treatment.
4. Relation between γ-globulin and tuberculin test.
5. Relation between γ-globulin and lympocytes.
6. Serum protein and prognosis of patient.
7. On serogram which is the simple method to express the value of serum protein, fraction.
The electrophoretin analysis of serum protein is very important method to know the extent of disease, prognosis and effect of chemotherapy.

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Results, which are obtained by electrophoretical method, have too many factors to be expressed in a simple manner. At least, three factors must be considered in the explanation of electrophoretic results; they are: 1) there are four or five components to express serum protein fractions (Alb., α-Glob., β-Glob. and γ-Glob) or plasma fractions (serum components plus fibrinogen), 2) electrophoretic pattern must be disscussed from vorious points of view, nomely, an alternation in forms and mobilities from the regular plasma or serum components, or an appearances of unusual component, 3) it is difficult to comprehend the increase or decrease by sinply observing the numerical changes of protein fractions.
Agogram and Serogram, designed by K. Honda et al and H. Kanagami et al, are new excellent graphical expressions of electrophoretical serum protein components, taking into account factors 1) and 3) mentioned above. We disscussed Hond's Agogram and revised it and designed “Agogram”.
There are some differencess between these two expressions. a) “Agogram” uses percentage to express the electrophoretic values. Because, we can obtain only percentage of protein fraction directly from the pattern, but not each protein concentration (g/dl) as applied in Agogram. And it is one of the charactsristics of the electrophoresis that we can catch correlational ratios. of protein components. Moreover, it is liable to produce errors to convert percentage of fraction into concentration values of each components. b) Agogram express the values of increase or decrease of components. But normal protein fraction has each different level, and for example, when both φ and γ-Glob. increased 10%, Agogram will express the increase of both components in the same degree, in spite of the fact that percentagec in increase in φ-component is much larger than that in γ-Glob. Accordingly our “Agogram” expresses the ratio of increase or decrease calculated by the following formula:
A-B/A×100=Ratio of increase or decrease
A: value of normal subjects (%)
B: value of the material
We applied this “Agogram” in clinical use together with the electrophoretic pattern and the values of each components, and could make easier and clearer interpretation of the protein fluctuations of pre-and post-operative period, carcinomas and various liver diseases.

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Characters of Harkness' plasma proteih equilibrium factor, K^(H), was discussed from theoretical point of view and the results were summarized as follows:
1. Harkness have taken into account for his K^(H) only three fractions, albumin (A), total globulin (G), and fibrinogen (F). It was made clear, however, that K^(H) could be generalized to our K, in which all fractions of plasma proteins were taken into consideration, and K was dependent on only percent composition of plasma protein fractions, being defined as follows;
K=a^α_n·g^α_α·g^β_β·g^γ_γ·f^f_n
where a_n+α+β+γ+f_n=a+gα+gβ+gγ+f=1 and 100a, 100gα, etc. were percentage of A-fraction, α-G-fraction, etc., respectively, whose normal averages were expressed by an, α, etc., i. e. the set of exponent indices.
2. It was shown theoretically that K or K^(H) was maximum for normal plasma, and its deviation from the normal value, K_n, or K_n^(H), for pathological plasma always occured in the direction of diminution of the K value. Effects of analytical errors in fractionation upon K or K^(H) value were also discussed and Harkness' claim that K^(H) increased in initial stage of diseases, then decreased in later stage, was criticized.
3. In order to express the deviation of K from K_n, the author introduced a quantity, Q, deviation factor of plasma protein equlibrium, which was given as follows:
Q=∑ (deviation of each fraction (%) from its normal value)×(its rate of deviation)
It was shown, then, that K was a sort of geometrical mean with weighting factors of % composition of plasma protein fractions and Q was proportional to its variance. It seemed therefore unnecessary to assume a dissociable complex protein as Harkness has done and the use of Q, instead of K, was more reasonable and more convenient to indicate a change in state of plasma protein composition.
4. The constitution of exponent indices in expression in K, i. e. weighting factors for gemetrical mean, was discussed.
5. From the general aspects of multiple equilibrium systems, we concluded that Q was an index of the deviation of qualitative equilibrium state of plasma protein from normal standard state, assuming quantitative and qualitative equilibrium between each fractions, the former of which was given by total amount of plasma proteins.

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Measurements of electrophoretic mobilities have contributed much to our understanding of the nature of proteins and other biologically important substances. The techniques usually employed, however, make use of optical methods and require a large amount os substances. so that the method cannot at present be generally used.
In this paper an attempt is described to determine electrophoretic mobilities at low concentrations. Mobilities can be caluculated by determining average concentrations of solute in upper (ascending) and lower (descending) limbs by appropriate analytical methods after the isolation of the four sections of ordinary Tiselius-type electrophoretic cell.
Mobilities of desoxypentose nucleic acid of herring sperm were measured in phosphate buffer at pH 7.7 and ionic strength 0.2 in concentration range 0.5-0.005% by measuring ultraviolet absorption at 258mμ and found to be about -16×10^-5cm²/sec. volt, which agrees very well with those obtained by an optical method. In the case of E. coli bacteriophages T3 and T4, measurements were made at concentrations of about 10⁷-10⁸ phages/cc (about 10^-6%) by determining the number of phages by a plaque method and found to be about -5×10^-5cm²/sec. volt.
It may be concluded that this method is very useful especially in biological studies, though the errors are still larger in these experiments than in the usual optical electrophoretic measurements.

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1) Employing Heiderberger's method, the author studied quantitative precipicin reactions in electrophoretically simple antigen systems, (yeast polysaccharide, crystalline hens egg alubumin, crystalline horse serum albumine, bovine serum and pseudoglobulin, bovin thyroglobulin and Proteus X19 Systems).
2) The antibody/antigen ratio in equivalence zone obtained by the immunological method by means of succesive injection of a small quantity of antigen, was higher than that obtained by the normal immune method.
3) The reaction equations were characteristic in each of the antigens, I was able to divide them into polysaccharide, albumin, globulin and bacteria systems.
Generally, the ratio AbN/Ag N in the precipitate in equivalence zone showed a tendency to be larger the larger the molecular wight of the antigens.
4) Calculating the molecular ratio of specific precipitate in equivalence zone, by means of antibody N/antigen N which I measured, and also using the known molecular weight of antigen and antibody, we obtained the following results,
Crystalline hens egg albumin 2.7
Crystalline horse serum albumin 4.6
Bovine thyroglobulin 12.2
5) I found that antibody quantity calculated by quantitative precipitin method agreed with antibody quantity calculated by electrophoretic method, and we measured antibody quantity in immune serum globulin by two different methods.
The results were as follows.
Yeast polysauharide; 18.6-30.5%, crystalline hens egg albumin: 17.5-34.9, crystalline harse serum albumin; 25.4-34.1%, γ-pseudo globulin; 21.1%, and Thyroglobulin; 19.7%.

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