Electrophoretic Separation of Calcium-soluble Fraction of α-casein:II. Electron-microscopic Observation on Separation of κ-casein from α-casein and Paper-electrophoretic Study of Caseins of Cow's and Human Milk
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Changes of casein particles of α-casein, crude κ-casein, αR-casein, and a mixture of the latter two were observed electron-microscopically.1. α-Casein formed globular particles in a 0.009 M CaCl2 solution and was gradually aggregated at a concentration of 0.25 M of CaCl2.2. Crude κ-casein was aggregated only to a small extent even at 0.25 M of CaCl2, but was coagulated with rennin.3. αR-Casein was so outstanding as to be aggregated quickly at 0.009 M of CaCl2. When the concentration of CaCl2 was lower than that value, for example, 0.004 M, it was globular in appearance.4. The aggregation rate of a mixture of αR-casein and crude κ-casein (4+1) was a little lower than that of α-casein alone. It was found that κ-casein increased the stabillty of αR-casein colloids.Electrophoretic behavior and stability against calcium ion of caseins were compared between cow's and human milk in electrophoresis on paper.1. By paper-electrophoresis the casein of cow's milk was divided into three fraction, α-, β-and γ-caseins, and that of human milk into three fraction (I, II, and III) of equal quantity. In the presence of calcium chloride, the casein of cow's milk was divided into other three fractions probably containing κ, β and αR• γ complex each, and that of human milk into two fractions supposed to be (I+III) and II. Among the casin fractions of human milk, there was no one electrophoretically homogeneous with the κ fraction of the casein of cow's milk.2. After electrophoresis with a calcium-free buffer, the separated three casein fractions each of cow's and human milk were moved to the vertical direction by electrophoresis with a buffer containing CaCl2. Then, in the case of the casein of cow's milk, the κ-fraction was separated distinctly from the α-fraction, while the αR-fraction remained on the base line. In the case of the casein of human milk, however, all the three fractions moved toward the anode, but fraction II moved relatively slowly and was supposed to be more susceptible to calcium ion than the other fractions.3. All the three fractions of the casein of human milk seemed to be less sensitive to calcium ion and rennin than the casein of cow's milk.
- 公益社団法人 日本畜産学会の論文
公益社団法人 日本畜産学会 | 論文
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