The macromolecular components, constituting mitochondria, were analysed electrophoretically and turbidimetrically and following results were obtained.
1. Macromolecules, extracted by acid or alkaline media, were analysed electrophoretically. It seemed probable that there should be little basic proteins which were in salt-like combination with other macromolecular.
2. The macromolecules, which were extracted by alkaline, were complex with the isoelectric points about pH 4.5-5.0. It was supposed that the complex proteins constituting the Gel-phase of mitochondria were extracted in fhemselves, They are probably negatively charged within the cell, attracting a great deal of cations with them.
3. The macromolecules, obtained by acid extraction, were relatively simple one. The protein part of the complex protein constituting the Gel-phase were profably extracted. The mechanisms of conbination of these proteins with nucleic acids and lipids were not so simple as the synthetic complex coacervate, and not only the ionic force but also the secondary force of binding (i. e. van der Waals force or hydrogen bond) or the specific steric configuration of macromolecules were probably contributing much to such combination. However, the analysis in detail were remained to be studied in future.

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1) The daily change of the electrophoretic pattern of the silkworm blood from larval to pupal stage was examined. Three components (b₃, b₂, b₁) were present in the blood of the early period of the 5th instar as shown in the previous paper (AIZAWA, 1955), while from 4-5th day of the 5th instar to pupal stage, there appeared two components, which were densely stained (Figs. 1, 3). In the latter case, when the electrophoresis was performed with the diluted blood, three protein components could be clearly detected (Fig. 2). b₃ is the fastest moving component and it seems to be albumin. b₂ and b₁ are probably globulin. b₃ component decreased with the pupal age and finally disappeared, at earlier time in male than in female.
2) Comparison of the electrophoretic patterns was made by veronal, phosphate, citrate, borate or tris (hydroxymethyl) aminomethane buffer with the varying ion concentration and pH. The separation of the protein fractions with veronal buffer (pH 8.6, I=0.05) was better than with other buffers.
3) Comparison of staining, was examined using bromphenol blue, solar blue black and amido black. All dyes were suitable for the purpose. By sudan black staining, b₃ component was slightly stained (Fig. 4).
4) Paper strips were cut off from the electrophoresis paper of the jaundice-diseased blood at the regions of b₃, b₂+b₁ and the starting line as shown in Fig. 5. The virus was extracted with the distilled water and the injection experiments were performed. The virus amount was highest in b₂+b₁ fractions and it decreased in the fraction from near the starting line. The virus activity was scarecely shown in the fraction of b₃.
5) Any difference, except for quantitative one was not observed in the electrophoretic patterns of the blood between the normal and diseased larvae (both nuclear and cytoplasmic polyhedroses). On the contrary, the pattern of Galleria mellonella is, however, different from that of Galleria-adapted silkworm jaundice virus (Aizawa, unpub.).

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The separation of inorganic radioactive phosphate, contamined with nucleic acids, proteins or lipids by means of paper-electrophoresis or of partition method was undertaken, and the following results were obtained.
1. Inorganic radioactive phosphate contaminated with RNA, if it may be in soluble state or precipitated as insoluble form, could easily be separated by means of paper-electrophoresis.
2. Inorganic radioactive phosphate contaminated with proteins, could also be separated by paper-electrophoresis.
3. Various solutions were applied to separate the contaminated inorganic P³² from lecithine dissolved in ether and it was ascertained that, by the Hahn's method of extraction with N/10 HCl, almost contaminated P³² could be eliminated, though considerable portion of lecithine were lost at the same time. With 10% NaCl, less lecithine were lost, though the elimination of inorg-P³² were not so complete as with N/10 HCl.

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The interaction between ovalbumin and lecithin was investigated by electrophoretically. And it was established that the formation of lipo-protein complexes occur under certain conditions when both components are negatively charged. These interactions were investigated in the phosphate buffer at pH7.0, Γ/2 0.223, ovalbumin lecithin weight ratio 3/1. Always it depends on the condit of solvent and may result in precipitation, complex formation of even inhibition of the heat coagulation of protein.

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