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  • 標題: 濾紙電気泳動

検索結果 27件

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濾紙電気泳動の基礎的実験
  • 大川 公康, 渡部 東馬
  • 生物物理化学
  • Vol. 5 (1958) No. 1
  • 公開日: 2009年03月31日
12-17
濾紙電気泳動法に関するシンポジウム
155-182
蛋白質の濾紙電気泳動法
3-16
濾紙電気泳動法の応用(第1報)
116-122,139
The apparatus devised consists of two buffer vessels, two Ag(AgCl)KCl-electrodes, two electrode vessels, a horizontal plate, a cover, and a supporter frame-work for filterpaper.
A few basic experiments were performed by means of this apparatus.
The buffer used was veronal-acetate buffer at pH8.6.
Results:
1) Veronal-buffer was found incomparably best adapted for filterpaper-electrophoretic analysis of blood serum.
2) 15 hours' electrophoresis under the current of 2mA or so was found to be most appropriate.
3) 0.02cc of serum was sufficient for the purpose.
4) The same buffer could be used 5 times in succession without any practical disadvantage.
5) The result obtained was approximately identical with that obtained by the use of the classical Tiselius apparatus.
6) The serum values obtained in 10 normal persons averaged Alb. 59.0%, α1-Glob. 3.7%, α2-Glob. 5.9%, β-Glob. 10.8% and γ-Glob. 20.6%.
  
蛋白質の濾紙電気泳動の基礎的研究
167-179
About the filterpaper electrophoresis of proteins, we come to a conclusion as the following, from the result of experiment, ussing serum (plasma) proteins as trial material after studing the provision of experimentation, material of experimentation according to the method of the experimentation.
1. We find inportant condition in the position on which we put the trial material, how much to have an overdose of it, and how fresh to have it.
2. The quality of the filterpaper has a close relation with the result of electrophoresis of proteins. We find the good result in the filterpaper of Whatman No. 1, Schleicher & Schüll No. 2043 a, b or Toyo filterpaper corp. No. 51, 51a.
3. About to the condition of the electrophoresis, the voltage, the electric current and the time of the phoresis are concerned each other. As to decide strictly on these point, we find some deficult problem, but we know that the condition of the phoresis had decided naturally, if we have the fixed filterpaper and buffer.
4. We find the best conditioh in about 7cm in phoresis distance and in 100-110°C, 20 minutes in the method of the desiccate as the same as we find from the result of experiment as to the phoretic distance and the desiccate method.
5. 20 minutes are the best in the time of dyeing so for as Amido black 10B is concermed.
We think as if We will find some deference between Amido black 10B and B. P. B. dyeingin in the result of the some amount, but it is not only clear above mentioned writting in this point of view but it is also necessary to study in future.
  
濾紙電気泳動法の標準化に関する研究
  • 杉本 良一, 阿部 正和, 猪熊 孝治, 阿武隈川 栄子, 宮本 璋, 坂岸 良克, 中島 一男, 高田 蒔, 畑下 敏行, 天野 久夫, 篠原 玲子, 伊藤 斉, 三浦 勇夫, 森 文彦, 斉藤 慶子, 土屋 豊, 吉野 純男, 井上 信彌, 小高 光, 橋本 明, 有賀 槐三, 長谷 克, 清水 清忠, 金田 春雄, 小林 茂三郎, 朝倉 三郎, 有賀 瑳智子, 杭田 亭, 橘 敏也, 村井 俊介, 玉井 温子, 村上 素子, 幾島 明, 島尾 和男
  • 生物物理化学
  • Vol. 5 (1958) No. 3-4
  • 公開日: 2009年03月31日
181-194
濾紙電気泳動分析に用いるデンシトメーターの規格および検定法
  • 島尾 和男, 杉本 良一, 宮本 璋, 浅田 敏雄, 有賀 槐三, 土屋 豊, 小林 茂三郎, 幾島 明, 伊藤 斉, 橘 敏也, 阿部 正和
  • 生物物理化学
  • Vol. 6 (1960) No. 4
  • 公開日: 2009年03月31日
258-261
カイコ血液蛋白の濾紙電気泳動
  • 鮎沢 啓夫, 村井 貞彰
  • 生物物理化学
  • Vol. 4 (1958) No. 1-2
  • 公開日: 2009年03月31日
23-26
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.).
  
追加発言1.濾紙電気泳動法によるリポ蛋白質の問題点
35
自動温度制御式濾紙電気泳動装置
  • 牧 正文, 吉野 光子
  • 生物物理化学
  • Vol. 11 (1965) No. 2
  • 公開日: 2009年03月31日
199-203
濾紙電気泳動法の基礎と乾電池法について
  • 久志本 常孝, 窪田 秀昭, 本間 光正
  • 生物物理化学
  • Vol. 3 (1956) No. 2
  • 公開日: 2009年03月31日
121-123
Using a laminated dry battery for portable radio use as an electrical source, human serum and eggwhite solution are paperelectrochromatographically developed.
In case when paper of the size of 2×20cm is used, current required was only 0.2mA with our circuit and arrangement. Fairly good patterns were obtained and it was verified that a laminated dry battery is never worse than a high-class rectifier as far as proteins are separated.
  
濾紙電気泳動法の基礎と乾電池法について
  • 久志本 常孝, 窪田 秀昭
  • 生物物理化学
  • Vol. 3 (1956) No. 1
  • 公開日: 2009年03月31日
32-35
Acetylated Sudan black Bを用いた血清脂蛋白濾紙電気泳動法のPre-staining Procedureについて
  • 伊藤 斉, 三浦 勇夫, 森 文彦, 石原 幸夫, 開沢 茂雄, 里和 宏
  • 生物物理化学
  • Vol. 6 (1960) No. 4
  • 公開日: 2009年03月31日
249-253
Paper electrophoresis is one of the most convenient methods for the study of serum lipoproteins. In spite of vast amounts of papers published, there is still many difficulties in the staining prncedure of lipid moiety of lipoprotein, e. g. poor staining, long time pecquired for staining, procedure and strong adsorption of dye to the paper itself. The author tested the pre-staining procedure using acetyl sudan black B prepared by the method of Lillie and Burtner. 0.1ml of saturated solution of the dye in ethanol was added to 1.0ml of serum before application of the serum on filter paper. Both alpha and beta lipoproteins migrate in a usual manner and appear much clear as blue zones against a white background.
Examination on the duration of staining, amount of sample, duration of electrophoresis the authors found that the best results could be obtained under the following conditions: buffer; veronal pH, 8.6; ionic strength 0.05; potential gradient; 10volt/cm; amount of sample 0.025-0.035ml/1.5cm; duration of electrophoresis 2-3 hours.
Comparing with Swahn's original method, pre-staining procedure reported here was foud to be better in reproducibility, time and cost.
  
濾紙電気泳動法に於ける分画別抽出法に関する研究
  • 橘 敏也, 村井 俊介, 玉井 温子, 村上 素子
  • 生物物理化学
  • Vol. 6 (1959) No. 1
  • 公開日: 2009年03月31日
63-71
In view of the complexity and inaccuracy of densitometery now in use, we adopted a fractional elution method as a substitute for it and made basic studies on the same with the following results:
1. Pigments are completely extracted from pieces of filter paper with 5-10cc of N/100 NaOH solution in 30 minutes at room temperature. The extinction of the extract and the amount of serum added show a linear relationship.
2. The color tone of the extract, which in prepared by removing bromphenol blue (BPB) or Amidoschwarz 10B (AS) from filter paper with N/100 NaOH solution, fades away with the passage of time; this phenomenon is especially remarkable in the extract which is prepared by removing BPB from filter paper with the said solution. Since the tendency of the color tone to fade away is true of each fraction of serum protein, no significant differences take place at least for 5 hours when the percentage of protein in serum is calculated.
3. The maximum resorption wavelengths of the extracts which are prepared by removing BPB and As from filter paper with N/100 NaOH solution are 570 and 620mμ.
4. When measurement is made by only an individual according to this method, its reproductivity is considerably high in each serum of healthy subjects and cases of nephrosis and liver cirrhosis.
5. Even when this method is performed on different individuals, it shows a reproductivity equal to that of the Tiselius method.
6. By this method we followed great changes in serum protein in cases of nephrotic syndrome that were produced during a short time by a large dosage of predonine.
  
各種血清Lipoproteinの超遠心分析とその濾紙電気泳動像
  • 山口 康夫, 中川路 慶一, 坂部 日出男, 秋元 真太郎, 関谷 昭
  • 生物物理化学
  • Vol. 5 (1958) No. 2
  • 公開日: 2009年03月31日
69-71
52-55
In the technique of Paper-electrophoresis, the size of the serum sample is an important factor, because a linear relation between protein concentration and densitometer reading depends upon it considerably.
While the original technique of applying the serum to an electrophoresis paper by a micropipet requires a skill acquired only by repeated practice, the use of an applicator strip which was used in this experiment, makes it easy to apply a constant amount of the serum sample. Furthermore, the above mentioned technique presents a well-separated pattern of serum protein, the separation of α1- and α2-globulin fractions being especially distinct.
The standard errors of the fractions are smaller compared with those by the micropipet method.
  
濾紙電気泳動法の基礎的研究
  • 猪熊 孝治, S. Y. Duer, 仲西 クキ子, 阿部 正和
  • 生物物理化学
  • Vol. 3 (1956) No. 1
  • 公開日: 2009年03月31日
10-15
As a part of our fundamental studies on paper electrophoresis we here present our views regarding selection of the two methods of paper electrophoresis, the Grassmann and the Flynn method. The filter paper used was Whatman No. 1, the stain, Amido Black 10 B.
Ten essentially normal human sera were used, and the results from both methods were almost identical, although differing in minor details. It is these minor differences that we wish to consider here.
(1) With the electrophoretic time being the same for both methods, the length of the electrophoretic migration was longer for the Grassmann method than for the Flynn method. This may be due to the movement of the buffer toward the center of the paper, as a result of the evaporation from the surface of the paper.
(2) The position of γ-globulin with the Flynn method was always on the negative side of the line of origin (electroosmosis), but with the Grassmann method it was consistently on the positive side. This, also, we consider is due to the flow of the buffer to compensate the evaporation loss.
(3) The protein adsorbed at the line of origin was more marked for the Flynn method than for the Grassmann method. We are now considering a way to eliminate this defect in the Flynn method. In order to observe the tailing of the albumin, therefore, the Grassmann method is more convenient.
(4) The reproducibility of both methods, as compared to free electrophoresis was not very good, owing to the evaporation from the paper and also to the sagging of the paper in the Grassmann method.
(5) From the above it is concluded that although the Grassmann method is more popularly used, the Flynn method when properly handled is far from being inferior to the former method.
  
253-265
Paper electrophoretic studies of serum protein iu the acidic Mc Ilvaine's buffer (pH 2.4 to 6.0) were carried out, using the open horizontal method. Further, the reproducible paper electrophoresis technique at pH 4.4 and the subsequent quantitative methods were reported.
The following results were obtained.
1. The acidic protein in serum, named M, is separated only between pH 4.8 and 4.0. At pH 4.8 and above, serum protein is separated into three fractions, namely, A, B1 and B2; no acidic protein is observed. At pH 3.6 and beneath, , serum protein is not separated in any fraction, and distributed only as a long and diffuse tailing on the cathodic part of paper.
2. Serum fractions at pH 4.4 are named M1, M2, A and B from the anodic components. B, having no electric charge at pH 4.4, is displaced only by the buffer flow. M1, M2 and A migrate to the anode with the apparent mobilities in this order, but the migration of A is very small. B alone migrates to the cathode.
3. Under the constant voltage of 200V, the electrophoretic separation at pH 4.4 is markedly influenced by the ionic strength of buffer solution and electrophoresis hour, namely, 1) with lower ionic strength, M1, M2, A and B are so far well resolved but their zones are diffuse and blurred, and 2) with much higher ionic strength, and also in too longer electrophoresis hour, they come together on the central part of paper because the buffer flow and the ionic strength on paper are exceedingly large.
4. Serum should be applied at the places where A remains immobile after electrophoresis. It is because B fuses with A, when the applied volumes of serum are relatively large, and because the fast moving M1 and M2 are flowed back owing to the buffer displacement and superimposed on the other fractions, if the application points are on the more anodic part than the above mentioned places.
5. In the author's laboratory, electrophoretic runs are routinely carried out at 200V for 14-16 hours, using Mc Ilvaine's buffer of pH 4.4 and 0.2 which contains 3.29g of citric acid (1 hydrate) and 10.53g of sodium diphosphate (12 hydrates) in a litre of destilled water.
6. By amido black staining, M1 is stained only faintly, M2 weakly, A and B exceedingly densely. By PAS-staining, M1 and M2 are densely stained only in cases with increased mucoproteins. A and B, in general, are faint and diffuse. Therefore. these staining methods are inadequate for the quantitative densitometry of these fractions.
7. Sera from some representative dysproteinemias including liver cirrhosis, gastric cancer, acute myelocytic leucemia, nephrotic syndrome and exudative pleuritis were run at pH 4.4 and fractionated. Subsequently, serum fractions and their protein-bound hexoses were chemically determined and compar ed.
8. The improved preparative electrophoresis by paper strips (Yamaguchi) is proved to be valuable for the clinical observation of serum pH 4.4 as well as for the further investigation of M1 and M2 fractions.
  
人血清蛋白の濾紙電気泳動法の基礎的研究
221-231
A systematic studies of the electrophoresis technique of human serum proteins (in sodium barbiturate buffer at pH 8.6) using the open horizontal method ware carried out.
1. During electrophoresis, two kinds of the buffer flow occur on paper surface, one of which heads for the cathode on account of the electroendosmosis. The other one goes to the central part of paper from both of the anodic and cathodic buffer vessels in order to compensate for the relative dryness which occurs owing to the evaporation during electrophoresis. The apparent buffer flow on paper surface is the algebraic sums of these two kinds of buffer flow. The equlibrum points (zero points) of buffer flow are generally located on the cathodic part of the horizontal portion of paper.
2. These equlibrium points, however, displace to the central part of paper as voltage, ionic strength and electrophoresis hour incerease. It is because, in these cases, the buffer flow due to the evaporation augments more rapidly than the one due to the electroendosmosis.
3. The buffer flow on the more anodic part than the equlibrium points heads for the cathod and inversely on the more cathodic part. Their dimensions are proportional to the distances from the equlibrium points of buffer flow.
4. On account of the buffer flow on paper, 1) the electrophoretic patterns are blurred, especially on the anodic part of paper, and displaced, as a whole, to the anodic or cathodic parts, leaving some extent of tailing on paper. This is disadvantageous for the precise determination of serum fractions because one fraction may be superimposed on the other's talings.
5. As the buffer solution displaces under the continuous evaporation during electrophoresis, the ionic strength varies throughout on paper. To detect the variations of ionic strength, accumulated amounts of electrolytes on the dried papers, were examined by the high-frequency papyrography The ionic strength is proved to be small where the buffer flow is large. So, the ionic strength on paper decreases in proportion to the increases of distance from the equlibrium points of buffer flow.
6. The time-migration relationship of B. P. B, stained Alb, is not linear but of inversely S-shaped curve, the formation of which is expounded to be due to the variations of ionic strength on paper.
7. The most well separated electrophoretic patterns are obtained when serum is applied on the equlibrium points of buffer flow. It is because the applied serum migrates on the paper with relatively high ionic strength and relatively small buffer flow.
8. In drying papers, the electrophoretically separated fractions are displaced owing to the water displacement due to the evaporation.
9. The paper electrophoretic mobilities are only approximate in both of the closed and open method electrophoresis because the changes of buffer flow and ionic strength during electrophoresis, and the water displacement in drying papers do not take place uniformly on paper.
  
超遠心的に分画した血清lipoproteinの濾紙電気泳動ならびに脂質構成に関する研究
  • 八杉 忠男, 中原 一実, 高橋 隆熙, 成宮 準一, 波多野 幸子, 本間 六雄
  • 生物物理化学
  • Vol. 6 (1959) No. 2
  • 公開日: 2009年03月31日
123-126