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The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.)

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Abstract

A fraction of highly purified prolamellar bodies was isolated from etioplasts of wheat (Triticum aestivum L. cv. Starke II, Weibull), as previously described by Ryberg and Sundqvist (1982, Physiol. Plant., 56, 125–132). Studies on the protein composition revealed that only one major polypeptide of an apparent molecular weight of 36000 is present in the fraction of prolamellar bodies. This polypeptide was identified as the NADPH-protochlorophyllide oxidoreductase. The highest specific activity of the enzyme in etiolated leaf tissue was confirmed to be in the fraction of prolamellar bodies.

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Abbreviations

PChlide:

protochlorophyllide

PLB:

prolamellar body

PT:

prothylakoid

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Authors and Affiliations

  1. Botanisches Institut, Christian-Albrechts-Universität, Olshausenstrasse 40, D-2300, Kiel, Federal Republic of Germany

    Katayoon Dehesh

  2. Botanical Institute, Department of Plant Physiology, University of Göteborg, Carl Skottsbergs Gata 22, S-413 19, Göteborg, Sweden

    Margareta Ryberg

Authors
  1. Katayoon Dehesh
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  2. Margareta Ryberg
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Dehesh, K., Ryberg, M. The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.). Planta 164, 396–399 (1985). https://doi.org/10.1007/BF00402952

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  • DOI: https://doi.org/10.1007/BF00402952

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