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

Planta ·Vol. 164 ·No. 3 ·1985-06-00 ·Pages 396-9

Dehesh K, Ryberg M

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.

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Dehesh K

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

Ryberg M

References (13)

13 references, click to expand

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Article Info

Journal

Planta

Abbr.

Planta

ISSN

0032-0935

DOI

10.1007/BF00402952

Published

1985-06-00

Pages

396-9

Language

English

Region

Germany

NLM ID

1250576

External Links

PubMed source DOI: 10.1007/BF00402952 View journal details

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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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