The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.) |
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| Authors: | Katayoon Dehesh Margareta Ryberg |
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| Institution: | (1) Botanisches Institut, Christian-Albrechts-Universität, Olshausenstrasse 40, D-2300 Kiel, Federal Republic of Germany;(2) Botanical Institute, Department of Plant Physiology, University of Göteborg, Carl Skottsbergs Gata 22, S-413 19 Göteborg, Sweden |
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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.Abbreviations PChlide
protochlorophyllide
- PLB
prolamellar body
- PT
prothylakoid |
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| Keywords: | NADPH-protochlorophyllide oxidoreductase Prolamellar body Prothylakoid Triticum (prolamellar body) |
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