Transformation of photoinactive to photoactive protochlorophyllide in isolated prolamellar bodies of wheat (Triticum aestivum) exposed to low pH and ATP-Reference-Cited by-同舟云学术

Transformation of photoinactive to photoactive protochlorophyllide in isolated prolamellar bodies of wheat (Triticum aestivum) exposed to low pH and ATP

Published:1987-06 Issue:2 Volume:70 Page:155-162
ISSN:0031-9317
Container-title:Physiologia Plantarum
language:en
Short-container-title:Physiol Plant

Author:

Grevby Cecilia,Ryberg Margareta,Sundqvist Christer

Publisher

Wiley

Subject

Cell Biology,Plant Science,Genetics,General Medicine,Physiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3054.1987.tb06125.x/fullpdf

Reference26 articles.

1. Restoration of A P657-647 form from P645-638 in extracts of etiolated primary bean leaves

2. The function of proteases during the light-dependent transformation of etioplasts to chloroplasts in barley (Hordeum vulgare L.)

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

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1. The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays );European Journal of Biochemistry;2002-04-22

2. ADP/ATP and protein phosphorylation dependence of phototransformable protochlorophyllide in isolated etioplast membranes;Photosynthesis Research;2000

3. Accumulation of Phototransformable Protochlorophyllide is Controlled by Protein Phosphorylation — A Hypothesis;Photosynthesis: Mechanisms and Effects;1998

4. The combined effects of acidification stress and kinetin on chlorophyll content, dry matter accumulation and transpiration coefficient inSorghum bicolor plants;Biologia plantarum;1994-01-01

5. Protochlorophyllide Reductase: A Key Enzyme in the Greening Process;Pigment–Protein Complexes in Plastids;1993