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Isolation and purification assay of ex vivo photosystem II D1 protein toward integrated biointeraction analysis

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Abstract

Protein extracts of photosystem II were prepared from leaf chloroplasts of different plant species by fast and nondenaturing methods. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blot analysis of the proteins obtained showed that the extracts were enriched by D1 proteins, which appeared putatively in association with the 33-kDa oxygen-evolving-complex subunits. In further isolation steps D1 proteins were purified using salt-gradient chromatography (fast protein liquid chromatography) and characterized by western blot and mass spectrometry.

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Acknowledgements

This study was supported financially by the Federal Ministry of Education and Research, grant no. 02WU0328, and the Caesar Foundation, Bonn, Germany.

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Authors and Affiliations

  1. Caesar Foundation, Ludwig-Erhard-Allee 2, 53175, Bonn, Germany

    B. Muktiono & C. Cerboncini

  2. IMBIO, University of Bonn, 53115, Bonn, Germany

    C. Schulten & H. Schnabl

  3. GKSS Research Center, 21502, Geesthacht, Germany

    J. Gandrass & A. Prange

  4. Residue Analysis Veterinary Institute, 26121, Oldenburg, Germany

    O. Heemken

Authors
  1. B. Muktiono
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  2. C. Schulten
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  3. O. Heemken
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  4. J. Gandrass
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  5. A. Prange
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  6. H. Schnabl
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  7. C. Cerboncini
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Correspondence to B. Muktiono.

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Muktiono, B., Schulten, C., Heemken, O. et al. Isolation and purification assay of ex vivo photosystem II D1 protein toward integrated biointeraction analysis. Anal Bioanal Chem 390, 1195–1202 (2008). https://doi.org/10.1007/s00216-007-1781-2

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  • DOI: https://doi.org/10.1007/s00216-007-1781-2

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