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Location and quantification of metal ions in enzymes combining polyacrylamide gel electrophoresis and particle-induced X-ray emission

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Abstract

A method is presented to identify and determine the relative amounts of protein-bound metal ionsin situ. Proteins or their subunits are directly scanned by a collimated proton beam of 3 MeV energy, and the characteristic X-rays produced are detected. The determination of Fe content of an iron-sulfur protein (HiPiP), as well as the Fe and Ni analysis of the hydrogenese fromThiocapsa roseopersina, have shown the feasibility of this technique.

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Authors and Affiliations

  1. Central Research Institute for Physics, Hungarian Academy of Sciences, PO Box 49, H-1525, Budapest 114, Hungary

    Zoltán Szökefalvi-Nagy & István Demeter

  2. Institute of Biophysics, Biological Research Center, Hungarian Academy of Sciences, PO Box 521, H-6701, Szeged, Hungary

    Csaba Bagyinka, Kornél L. Kovács & Huen Le Quynh

Authors
  1. Zoltán Szökefalvi-Nagy
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  2. Csaba Bagyinka
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  3. István Demeter
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  4. Kornél L. Kovács
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  5. Huen Le Quynh
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Szökefalvi-Nagy, Z., Bagyinka, C., Demeter, I. et al. Location and quantification of metal ions in enzymes combining polyacrylamide gel electrophoresis and particle-induced X-ray emission. Biol Trace Elem Res 26, 93–101 (1990). https://doi.org/10.1007/BF02992662

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  • DOI: https://doi.org/10.1007/BF02992662

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