Rabbit's serum which were suffered from allergic myocarditis, pleurisy, peritonitis, erythron-allergy (MAEKAWA) and lymphon-allergy (MAEKAWA) by each organ phosphatide were studied by electrophoresis. It was analysed allergic antibody and immune antibody in those rabbit's serum. The results were summerrized as follows. In gamma globulin of rabbits sensitized with a mixture of organ phosphatide and oxen serum, it was less than with oxen serum only and some of them showed T-peak in electrophoresis. It will be probably allergic antibody. When rabbits sensitized with a mixture of organ phosphatide and egg albumin, they had gama globulin less than the rabbits sensitized with formalysed egg albumin only. This reason as follows. When rabbits were sensitized with oxen serum or formalysed egg albumin only, immune antibody was produced in the rabbits. While, with a mixture of organ phosphatide and oxen serum or of organ phosphatide and egg albumin, the rabbits had allergic antibody. Allergic antibody adhered in tissue but immune antibody existed in serum. Therefore, it is natural that gamma globulin was little in the rabbits which had allergic phenomenon, because allergic antibody mainly will adhere in tissue and partly exist in serum. Alpha globulin was more recognized in serum of rabbits sensitized with a mixture of organ phosphatide and oxen serum than healthy rabbits and rabbits sensitized with oxen serum only. It is presumed that alpha globulin takes part in allergic antibody.

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1) The crossreaction of various kinds of tissue proteins against the liver protein antibody has been investigated by a quantitative precipitin method.
(a) The protein fraction of respectively liver, lymphnode and spleen has been found to crossreact against the antibody in a descending order of reactivity.
(b) Thyroglobulin and lens protein showed no precipitin reaction against the antibody.
2) The protein fraction of liver prepared by successive salting out with sodium sulfate has been investigated by an electrophoretic method.
The C₃ fraction (0-14g/dl) shows a simple peak, C₂ fraction (14-28g/dl) shows several peaks, while C₁ fraction a single peak of obture tapering.
If globulin peaks are respectively named G₁, G₂, G₃ in order of mobility, the mobility of C₃ fraction apparently corrends to G₂ peak, and that of C₂ fraction to peaks G₁ and G₃, while that of C₁ fraction to either G₂ or G₃.
3) The enzyme activity has been measured in respective liver protein fraction, and the C₃ fraction was shown to contain catalase and peroxidase, the C₂ fraction to contain esterase and cathepsin. The C₁ fraction to contain less enzyme than the C₃ and C₂ fractions.
The precipitate of C₂ and anti C₂ rabbit serum showed 30% esterase activity as against the original C₂ esterase activity.
4) The anti serum-γ-globulin antibody has been discovered to crossreact against the protein of respectively lymph node, spleen, and liver in descending order of reactivity, and C₃, C₂, C₁ fraction in order of reactivity.
5) The lens protin evidenced two separate major peaks and another small fast-moving one when treated by an electrophoretic method. The faster moving of the two major peaks apparently represented α crystalline while the slower one did β crystalline.
6) The antibody N produced in various kinds of the tissue protein extracted from the organs of a rabbit that was immunized by means of intravenous injection was discovered to exist in bonemarrow, spleen, lymph node, liver, lung, kidney respectively in order of antibody reactivity.
7) The antibody N produced in the popliteal lymph node in a rabbit immunized by a foot-pad injection was found to be 1.7-2.2 times greater in amount than serum antibody.
The antibody N remained in lymphatic cells laved with saline, and the antibody N of lymphatic saline soluble protein was shown to exist in greater amount than that of mitochondria and nucleus fraction by a quantative precipitin method.
8) It is inferred from the above that the liver protein, which the production of the serum albumin has been attributed, contains an extremely small amount of the component which has been ascertained to have the mobility identical with that of serum albumin by an electrophoretic method, and the reticuloendotherial system which has been believed to be responsible for the production of the serum γ globulin has a component crossreactive to the serum γ globulin, while the tissue antibody increase in the reticuloendothelial system, especially in the lymphatic system through immunization.

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An electrophoretic study by means of the Tiselius apparatus, was made on the influence of Dicumarol on normal human serum protein fraction.
100-150mg of Dicumarl of was administered, orally, for three consecutive days, and the serum protein fractions were compared before and after administration of the drug.
Two significant changes were noted.
1) A decrease in serum total protein. Although clinically, liver function is said to be unaffected by a therapeutic dose of Dicumarol, it may be that together with the inhibition of the production of prothrombin in the liver, some other factors may be influenced by Dicumarol.
2) A decrease in β-globulin. The amount of prothrombin in the blood is only 0.02g/dl. Hence an average decrease of 6.16g/dl as obtained in this experiment cannot be explained solely by decrease in the prothrombin which is associated with the β-globulin. Mann and many other investigators, as opposed to Quick, report that Dicumarol influences other factors than prothrombin. Although we cannot as yet specify the factors involved, this experiment appears to support the former view. It is also reported by Muto et al., that a minute quantity (0.002g/dl) of Heparin causes an increase in the albumin fraction when measured electrophoretically. The explanation given by them is an interaction between the heparin and albumin. However, further experiments are necessary to give a definite conclusion on the cause of the β-globulin decrease, noted in this experiment.

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