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1997 Fiscal Year Final Research Report Summary

Structure-Function Analysis of One single Ferritin Molecule with Electron Microscopy

Research Project

Project/Area Number 08455378
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field 生物・生体工学
Research InstitutionNational Institute for Physiological Sciences (1997)
The University of Tokyo (1996)

Principal Investigator

NAGAYAMA Kuniaki  National Institute for Physiological Sciences, Ultrastructure Research, Professor, 生理学研究所, 教授 (70011731)

Co-Investigator(Kenkyū-buntansha) TAKAHASHI Takuya  National Institute for Physiological Sciences, Ultrastructure Research, Research, 生理学研究所, 助手 (70262102)
Project Period (FY) 1996 – 1997
KeywordsElectron microscopy / Ferritin / Structure-function relation / Single molecular analysis / Biophysics
Research Abstract

This research was planned to establish a functional assay for a single protein molecule. To recognize individual protein molecules, electron microscopy, which is the most prominent in the spacial resolving power, was employed. As the biological function recognizable with electron microscopy, we have chosen the iron-incorporation process conducted by ferritin molecules, which could store iron of up to 3500 atoms, easily identified with the mirosocpy, For the two-years research duration, following new findings were obtained.
1)A single molecular functional assay of iron-incorporatibility of ferritin is established with TEM and high resolution SEM
2)Ferritin molecules stably adsorbed onto silicon surface shows about 20% residual function on iron-incorporability compared with those in the solution phase
3)Low on high pH condition drastically impairs the iron-incorporation activity of ferritin molecules when stably adsorbed onto silicon surface
4)Anti-correction between the functional stability and the strength of adsorption is observed
5)Ferritin molecules transfered from the mercury surface to the carbon surface in keeping the array form can maintain the iron-incorporability up to 85%.
6)The closely packed array form of ferritin molecules are very stable in maintaing activity compared with those sparsely and randomly adsorbed on carbon surface.

  • Research Products

    (1 results)

All Other

All Publications (1 results)

  • [Publications] 永山国昭(編): "“Protein Array : An Alternative Biomolecular System" Advances in Biophysies Vol.34" 学会出版センター, 350 (1997)

    • Description
      「研究成果報告書概要(和文)」より

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Published: 1999-12-08  

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