Studies on the Interaction between α<sub>s1</sub>- and β-Caseins

DOI DOI オープンアクセス
  • YOSHIKAWA Masaaki
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
  • SUGIMOTO Etsuro
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
  • CHIBA Hideo
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University

書誌事項

タイトル別名
  • Studies on the interaction between .ALPHA.SI- and .BETA.-caseins.

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説明

The interaction of αS1-casein with β-, dephosphorylated β-, γ- and R-caseins was studied. It was proved by the sedimentation velocity experiments that αSl-casein formed a complex with each of these components at 25°C in the presence of 3mM CaCl2.<br> In the presence of 10mM CaCl2, β- and dephosphorylated β-casein prevented the precipitation of αS1-casein and gave micelle-like turbid solutions. However, γ- and R-caseins, fragments of β-casein, did not stabilize αS1-casein. It was concluded from these results that β-casein interacted with αS1-casein through its hydropholic region corresponding to R-casein and that hydrophilic region of β-casein was responsible for the stabilization of αS1-casein.

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詳細情報 詳細情報について

  • CRID
    1390001206468781696
  • NII論文ID
    130003525081
  • DOI
    10.1271/bbb1961.39.1843
    10.1080/00021369.1975.10861856
  • COI
    1:CAS:528:DyaE2MXlvFWms7k%3D
  • ISSN
    18811280
    00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
    • OpenAIRE
  • 抄録ライセンスフラグ
    使用不可

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