Organization of protochlorophyllide oxidoreductase in prolamellar bodies isolated from etiolated carotenoid-deficient wheat leaves as revealed by fluorescence probes-Reference-Cited by-同舟云学术

Organization of protochlorophyllide oxidoreductase in prolamellar bodies isolated from etiolated carotenoid-deficient wheat leaves as revealed by fluorescence probes

Published:2005-10 Issue:2 Volume:1716 Page:97-103
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Denev Iliya D.,Yahubyan Galina T.,Minkov Ivan N.,Sundqvist Christer

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference48 articles.

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2. Pigment–protein complexes in illuminated etiolated leaves;Oliver;Plant Physiol.,1982

3. The Pchlide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH:protochloriphyllide oxidoreductase;Apel;Eur. J. Biochem.,1980

4. Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts;Ryberg;Physiol. Plant.,1982

5. Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies;Ryberg;Physiol. Plant.,1986

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