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Analysis of Photosystem II Proteins by Two-Dimensional Electrophoresis

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Progress in Photosynthesis Research

Abstract

Photosystem II preparations with high rates of 02 evolving activity were first purified by solubilization with Triton X-100 of stacked (1) or unstacked (2) thylakoids. These PSII preparations contain an abundance of light harvesting complex (LHC) proteins as well as the PSII reaction center (RC) and the oxygen evolving complex (OEC). Solubilization of PSII preparations with 1-O-n-octyl-ß-D-glucopyranoside has been found to purify the PSII RC and OEC further from the LHC proteins (3–5).

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Author information

Authors and Affiliations

  1. Frasch Department of Biology, The University of Michigan, Ann Arbor, Mi, 48109, USA

    Leslie J. Baier, Neil R. Bowlby & D. Wayne

Authors
  1. Leslie J. Baier
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  2. Neil R. Bowlby
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  3. D. Wayne
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Editor information

Editors and Affiliations

  1. Division of Biology and Medicine, Brown University, Providence, RI, 02912, USA

    J. Biggins

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© 1987 Martinus Nijhoff Publishers, Dordrecht

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Baier, L.J., Bowlby, N.R., Wayne, D. (1987). Analysis of Photosystem II Proteins by Two-Dimensional Electrophoresis. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3535-8_28

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  • DOI: https://doi.org/10.1007/978-94-009-3535-8_28

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-8080-4

  • Online ISBN: 978-94-009-3535-8

  • eBook Packages: Springer Book Archive

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