Preparation of Luciferase-fused Peptides for Immunoassay of Amyloid Beta

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  • SAKONO Masafumi
    Department of Applied Chemistry, Faculty of Engineering, University of Toyama
  • ARISAWA Taiki
    Department of Applied Chemistry, Faculty of Engineering, University of Toyama
  • OHYA Takuma
    Department of Applied Chemistry, Faculty of Engineering, University of Toyama
  • SAKONO Naomi
    Department of Applied Chemistry and Chemical Engineering, National Institute of Technology, Toyama College
  • MANAKA Atsushi
    Department of Applied Chemistry and Chemical Engineering, National Institute of Technology, Toyama College

書誌事項

公開日
2021-05-10
資源種別
journal article
DOI
  • 10.2116/analsci.20scp19
公開者
社団法人 日本分析化学会

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説明

<p>An immunoassay, such as the enzyme-linked immunosorbent assay (ELISA), is an analytical method that utilizes the interaction of antigens and antibodies. Enzyme-labeled antigens require both molecular recognition by the antibody and enzymatic activity as a reporter. We designed and constructed an immunodetection system for amyloid beta peptides (Aβ) using an enzyme-labeled antigen expressed from Escherichia coli. Aβ(1–16) fused with renilla luciferase was prepared as the enzyme-labeled antigen. In the presence of this luciferase-fused peptide, the luminescence of coelenterazine-h was observed. The influence of the fusion with Aβ on the luminescence reaction was insignificant. Surface plasmon resonance analysis indicated that the interaction between the luciferase-fused Aβ and anti-Aβ antibody was sufficiently strong. In the competitive ELISA assay for Aβ detection using the luciferase-fused Aβ, the luminescence intensity decreased as the Aβ concentration increased.</p>

収録刊行物

  • Analytical Sciences

    Analytical Sciences 37 (5), 759-763, 2021-05-10

    社団法人 日本分析化学会

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