@article{oai:kpu.repo.nii.ac.jp:00004888,
 author = {三好, 正満 and Miyoshi, Masamitsu and 伊吹, 文男 and Ibuki, Fumio and 金森, 正雄 and Kanamori, Masao},
 journal = {京都府立大學學術報告. 農學, The scientific reports of Kyoto Prefectural University. Agriculture},
 month = {Oct},
 note = {κ-カゼインを三種の方法で調製し, 電気泳動, 超遠心分析, α_S-カゼイン安定化力等について調べた。尿素中における等電点はpH6.0であり, α_S-カゼインとは違うことが明確になった。S_<20,W>は尿素中で2.6&acd;3.8であり尿素が存在しないとpH8.0で14.4を示した。ヘキソースは1.5%, シアル酸は0.8%, リンは0.2%, チッ素は14%程度であった。DEAEセルロースクロマトグラフィーによって分画される前後でアミノ酸組成には変化がなかったが, α_S-カゼイン安定化力は分画後増大する傾向にあった。, κ-Caseins were prepared by the calcium ethanol method, the Sephadex method and the urea sulfuric acid method. Some important properties of κ-caseins were investigated using isoelectric focusing, starch gel electrophoresis, ultracentrifugation, chemical analysis, stabilizing test of α_S-casein, and rennin treatment. Isoelectric focusing established that κ-casein had its isoelectric point near pH6.0 in 6M urea, usually accompanied by a second peak around pH5.6. Ultracentrifugation, however, showed a single peak having a S_<20,W> value of 2.6-3.8 in the presence of 6M urea and of 14.4 in the absence of such dispersing reagents. Normal contents of hexose, sialic acid, phosphorus, and nitrogen were respectively about 1.5,0.8,0.2,and 14%. Relative patterns of amino acid composition were similar in all the κ-caseins. In addition, amino acid composition in intact κ-casein and in the further purified κ-casein which formed the second peak in DEAE cellulose chromatography were almost identical, indicating that the κ-casein of the first peak is not an impurity but is one of the components which formed the original κ-casein complexes. The ability of κ-caseins to stabilize α_S-casein in the presence of calcium increased when purified by DEAE cellulose chromatography.},
 pages = {128--134},
 title = {Studies on κ-Casein of Bovine Milk III : Some properties of κ-casein and its complex (Agricultural Chemistry)},
 volume = {23},
 year = {1971},
 yomi = {ミヨシ, マサミツ and イブキ, フミオ and カナモリ, マサオ}
}