The effect of carbon tetrachloride and benzene poisoning on the serum proteins of rabbits was investigated electrophoresis. In benzene poisoning the increase of β-globulin was observed, but in carbon tetrachloride poisoning the increase of α-globulin was obvions.
The ratio of β-lipoprotein to α-lipoprotein was increased in both of the poisoning. But this phenomena is not caused by the decrease of α-lipoprotein.
In carbon tetrachloride poisoning the decrease of albumin was remarkable.

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1.まむし毒中には電気泳動的に区別しうる成分が少くも6個含まれている。
2.まむし毒成分中でのフオスフオリパーゼAおよび溶血毒の分布をみるため次の二次元濾紙泳動法を試みた。
ブドー糖を3.5%に添加して等張としたpH8.6,μ0.05のベロナール緩衝液を用い,まむし毒を第一の次元(X方向)に泳動させ,この上に全血液,または血球をぬつて溶血をおこさせた後,第一の次元と直交する第二の次元(Y方向)に電場を加え,溶血して血球外へ出たヘモグロビンのみをこの方向へ泳動せしめる。
3.上記二次元濾紙泳動法によつてまむし毒中での溶血毒およびフオスフオリパーゼAの分布を明らかにした。溶血毒はまむし毒成分中易動度の最も小さい成分に伴つており,フオスフオリパーゼAはこれより易動度のやや早い成分に含まれている。

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In 1954, Kuroda³⁾ discovered that the intensity of the light passing through the flowing erythrocyte suspension is greater than that through the resting suspension and called this phenomenon the “streaming transparency”, introducing as a quantitative expression of the shape of erythrocyte^5-19).
The optical density (A) of the cytosoid⁴⁾, such as erythrocyte suspension, is generally expressed by the following equation²⁰⁾:
A=log{I₀/I_p+fI_s}, 0<f<1…(1)
where I₀ means the intensity of incident light, I_p is the light intensity passed through the medium, I_s is the light intensity scattered by the cytosoidal particles and f is the proportion of the scattered light received by the photoelectric tube to the total I_s. When the optical density of the flowing suspension is expressed by the following equation:
A'=log{I₀/I_p'+f'I_s'}…(2)
the streaming transparency is given by
A-A'=logI_p'+f'I_s'/I_p+fI_s…(3)
In the case of the particles which strongly scatter the light, the streaming transparency of the suspension, A-A', is larger than zero at the low particle concentration, because in the flowing state the increase of fI_s is superior to the decrease of I_p, namely, f'I_s'-fI_s>I_p-I_p'. However, it is smaller than zero at the high particle concentration in consequence of the mutual effect of opal glass action of layers in the suspension (Fig. 7, Table 2). The streaming transparency of erythrocyte suspension at the wave length except Soret band of hemoglobin belongs to this group (Fig. 9).
On the contrary, in the case of the particles which strongly absorb the light, the streaming transparency is smaller than zero at the low concentration of particle, because the decrease of I_p is superior to the increase of fI_s in the flowing state, namely, I_p-I_p'>f'I_s'-fI_s. And it becomes larger than zero at the high concentration as the result of the mutual effect of absorption among each layer of the suspension (Table 3). The streaming transparency of erythrocyte suspension at the wave length of Soret band belongs to this group (Figs. 11, 13). However, when the particles in the suspension do not scatter the light entirely, the streaming transparency of the suspension is always smaller than zero irrespective of the particle concentration (Fig. 12).

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The present paper deals with the proteins. to be extracted from human, placenta, which were studied by means of electrophoresis, determination of solubility against ethanol and immunochemical titration.
γ-Globulin from this tissue was successfully purified by ethanol fractionation method proposed by Cohn for plasma proteins, and compared immunochemically with γ-globulin prepared from pooled blood plasma.
The results obtained are as follows:
1) Normal placenta weighed approximately 400g. in wet weight, and its content of water and proteins were 84 and 12.2 per cent respectively. About one-fourth of total protein could be extracted by immersion of placenta slice overnight in water.
2) Electrophoretic analysis of the proteins extracted revealed four components having the same mobilities as those of serum albumin, α- β- and γ-globulins respectively. Considering the pattern observed in case of perfused placenta, the component, of the same mobility as γ-globulin was most likely derived from the tissue itself, while the other cpmponents were probably from contaminating blood.
3) Some changes in the electrophoretic pattern caused by autolysis were described.
4) 20 per cent ethanol precipitated all antibodies tested, and this fraction was further purified using the method 9 proposed by Cohn.
5) γ-Globulin thus purified from placenta manifested a little higher antibody titers for several antigens examined than those of γ-globulin preparation from blood plasma.

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In an attempt to examine changes in hemoglobin, the erythrocyte count, the total protein and serum protein anemia was induced in rabbits by taking a large amount of blood once, a moderate amount of blood every other day and a small amount of blood every day by bloodletting. Serum protein was separated into fractions by means of paper electrophoresis.
1. The intensity of anemia was in the following order: a great amount of blood>a moderate amount a small amount In the beginning of bloodletting anemia took place rapidly and then slowly. The decreasing rate of the total protein was lesser than that of anemia. When a small amount of blood was taken by bloodletting, the total protein showed an increase over the pre-operative value during bloodletting.
2. Changes in the protein fractions occurred immediately after bloodletting. These changes became more marked 24 hours after bloodletting. There was a decrease in the albumin fraction even when any of the methods for bloodletting was used. The decrease in the albumin fraction constituted major changes in protein. The decreasing rate of the albumin fraction was not always proportional to the intensity of anemia. The return of the albumin fraction to normal levels required a long period of time.
3. Any of the methods for bloodletting produced an increase in α₁-globulin and α₂-globulin. They made up for the initial decrease in the albumin fraction.
4. During the recovery of anemia a striking increase in β-globulin was observed even when any of the methods was employed for bloodletting.
5. γ-globulin showed an increase when a decrease in albumin lasted for a long time. It seemed as if the former increase compensated for the latter decrease, but γ-globulin rather decreased when anemia was small in intensity.

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