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 C
3 fraction (0-14g/dl) shows a simple peak, C
2 fraction (14-28g/dl) shows several peaks, while C
1 fraction a single peak of obture tapering.
If globulin peaks are respectively named G
1, G
2, G
3 in order of mobility, the mobility of C
3 fraction apparently corrends to G
2 peak, and that of C
2 fraction to peaks G
1 and G
3, while that of C
1 fraction to either G
2 or G
3.
3) The enzyme activity has been measured in respective liver protein fraction, and the C
3 fraction was shown to contain catalase and peroxidase, the C
2 fraction to contain esterase and cathepsin. The C
1 fraction to contain less enzyme than the C
3 and C
2 fractions.
The precipitate of C
2 and anti C
2 rabbit serum showed 30% esterase activity as against the original C
2 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 C
3, C
2, C
1 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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