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Development of a homegeneous immunodiagnostics system utilizing luminescence wavelength transformation by energy transfer

Research Project

Project/Area Number 08555199
Research Category

Grant-in-Aid for Scientific Research (A)

Allocation TypeSingle-year Grants
Section展開研究
Research Field 生物・生体工学
Research InstitutionThe University of Tokyo

Principal Investigator

NAGAMUNE Teruyuki  Univ.Tokyo, Dept.Chem.& Biotechnol., Professor, 大学院・工学系研究科, 教授 (20124373)

Co-Investigator(Kenkyū-buntansha) KITAYAMA Atsushi  Univ.Tokyo, Dept.Chem.& Biotechnol., Resesarch Associate, 大学院・工学系研究科, 助手 (70270882)
UEDA Hiroshi  Univ.Tokyo, Dept.Chem.& Biotechnol., Lecturer, 大学院・工学系研究科, 講師 (60232758)
Project Period (FY) 1996 – 1997
Project Status Completed (Fiscal Year 1997)
Budget Amount *help
¥8,400,000 (Direct Cost: ¥8,400,000)
Fiscal Year 1997: ¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 1996: ¥5,700,000 (Direct Cost: ¥5,700,000)
KeywordsHomogeneous immunoassay / Fluorescence Resonance Energy Transfer / Transformation of Luminescence Wavelength / Chimeric Protein
Research Abstract

To develop a sensitive homogeneous immunoassay, verification of a homogeneous immunoassay principle which utilize luminescence energy transfer and transformation of luminescence wavelength, was attempted.
When variable amount of fluorescent labeled antibody was mixed with chimeric protein A-Vargula luciferase and substrate luciferin, marked red shift in luminescence spectre possibly due to efficient luminescence energy transfer was detected. It was also detectable with a microtiter well-type luminometer with long pass filter unit. The amount of labeled antibody correlated well with the extent of luminescence with red-shifted wavelength, which suggests the feasibility of new luminescent homogeneous immunoassay. To obtain better sensitivity in the assay, a novel chimeric protein of protein G-Vargula luciferase was made and shown to have 2-fold sensitivity than protein A-luciferase. The result thus implies a possibility of new antigen detection method employing epitope-tagged luciferase and fluorescent-labeled antibody.

Report

(3 results)
  • 1997 Annual Research Report   Final Research Report Summary
  • 1996 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] S.Hayakawa et al: "X-ray microprobe system for XRF analysis and spectroscopy at SPring-8 BL39XU" J.Synchrotron Rad.5. (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Y.Maeda and T.Nagamune: ""Truncation of Vargula Luciferase Still Results in Retention of Luminescence"" J.Biochem.119. 601-603 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Y.Maeda and T.Nagamune: ""Engineering of Functional Chimeric Protein G-Vargula Luciferase"" Anal.Biochem.249. 147-152 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] T.Nagamune, Y.Maeda, E.Suzuki and H.Ueda: ""Chimeric Luciferase with Antibody Binding Affinity Engineered for Immunological Assay System"" J.Grad, Sch.Fac.Eng., Univ.of Tokyo. A-34. 92-93 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Yumi Maeda: "Engineering of Functional Chimeric ProteinG-Vagula Luciferasc" Anal.Bitchem.249. 147-152 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] Yumi Maeda: "Truncation of Vargula Luciferase Still Results in Retertion of Luninescence" J.Biochem. 119. 601-603 (1996)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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