Disc-電気泳動法によるメダカ卵タンパク質の分画(予報)
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Utilizing the recently developed electrophoretic supporting medium, acrylamide gel, proteins extracted from eggs of the Japanese Medaka, Oryzias Latipes, at various stages in development have been fractionated by disc-electrophoresis. Oryzias eggs were selected periodically during their six day development at 30℃ (Stages 11 through 33). Whole eggs were homogenized in cold deionized water or 1/7.5 M KCl and centrifuged for 40 minutes at 10,000 rpm at 3℃ yielding a supernatant of 6 equivalent eggs per 0.2ml. Electrophoresis was performed as described by Ornstein and Davis (1962). A constant current of 4 mA per gel (10cm×7mm) was applied for approximately 2.5 hours in a tris-glycine buffer system (pH 8.7) containing a trace of Bromphenol Blue as a standard. The gels were stained with Amido Black 10B. After destaining in 7% acetic acid, the results were recorded photographically and by scanning photometrically. The mobility of each band was expressed in terms of the BPB front (distance from origin to band over distance from origin to front). Conversion of actual mobilities to relative mobilities (Rm Values) largely removes inter-gel variability. At least eight protein bands are visible in a typical photometric record of a fractionated aqueous extract from first day eggs (Fig. 1). Those bands which are present in the highest concentrations (1, 3 and 4) also exhibit relatively low mobilities. Comparisons of water and KCl extractable proteins taken from whole eggs at various stages of development indicate that the total amount of water soluble proteins markedly decreases as development proceeds. In addition, aqueous fraction Rm 0.35 apparently disappears after the third day while the KCl fraction with comparable Rm values (0.32, 0.34) persists through the fifth day (Fig. 2). An evaluation of the similarity of these KCl and water soluble fractions must take account of changes in their solubilities due to combination with lipids. We are presently trying to establish if any of the Oryzias egg fractions are phosphoproteins.
- 社団法人日本動物学会の論文
- 1964-04-15
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