Preparation of Antibody-Coupled Liposomes Containing Horseradish Peroxidase as a Marker Molecule

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Horseradish peroxidase (HRP) was encapsulated in liposomes prepared by an extrusion technique. The liposomes were coupled covalently to anti-rabbit IgG using N-hydroxysuccinimide ester palmitic acid as a component of liposomes. The number of encapsulated HRP molecules per liposome was about 800. A large portion of HRP was encapsulated inside the liposomes for about one week at 4°C. The catalytic activity of HRP was measured by a luminol chemiluminescence (CL) method and was found to be almost constant during storage. The CL intensity per antibody in the detection of HRP encapsulated in the antibody-coupled liposomes was 125-times greater than that of HRP conjugated directly to the antibody.

収録刊行物

  • Analytical sciences : the international journal of the Japan Society for Analytical Chemistry

    Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 15(4), 349-352, 1999-04

    社団法人 日本分析化学会

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各種コード

  • NII論文ID(NAID)
    10002419375
  • NII書誌ID(NCID)
    AA10500785
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09106340
  • NDL 記事登録ID
    4712405
  • NDL 雑誌分類
    ZP4(科学技術--化学・化学工業--分析化学)
  • NDL 請求記号
    Z54-F482
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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