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Studies on κ-Casein of Bovine Milk III : Some properties of κ-casein and its complex (Agricultural Chemistry)
https://kpu.repo.nii.ac.jp/records/4888
https://kpu.repo.nii.ac.jp/records/48880cfb368f-6e91-41c2-8610-7752b8c2df9a
名前 / ファイル | ライセンス | アクション |
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KJ00000078887.pdf (530.0 kB)
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Item type | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-02-20 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Studies on κ-Casein of Bovine Milk III : Some properties of κ-casein and its complex (Agricultural Chemistry) | |||||
その他(別言語等) | ||||||
その他のタイトル | 牛乳のκ- カゼインに関する研究 III : 二, 三の性質(農芸化学部門) | |||||
言語 | ja | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ | departmental bulletin paper | |||||
著者 |
三好, 正満
× 三好, 正満× 伊吹, 文男× 金森, 正雄 |
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抄録(日) | ||||||
内容記述タイプ | Other | |||||
内容記述 | 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∿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。 | |||||
言語 | ja | |||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | 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. | |||||
言語 | en | |||||
書誌情報 |
ja : 京都府立大學學術報告. 農學 en : The scientific reports of Kyoto Prefectural University. Agriculture 巻 23, p. 128-134, 発行日 1971-10-15 |
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雑誌書誌ID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN00062275 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 00757373 |