Literature DB >> 6456902

Sub-etioplast localization of the enzyme NADPH: protochlorophyllide oxidoreductase.

C Lütz, U Röper, N S Beer, T Griffiths.   

Abstract

The membranes from oat etioplasts have been separated by sucrose density gradient centrifugation into a heavy fraction of density 1.20 mg/ml (prolamellar body fraction) and a light fraction of density 1.12 mg/ml (prothylakoid fraction). The light fraction was shown to be enriched in protein, protochlorophyllide and the chloroplast enzyme CF1-ATPase, but to be deficient in saponins. In the electron microscope this fraction appeared as swollen vesicles. In contrast the heavy fraction appeared considerably enriched in crystalline, tubular material and was on analysis found to contain most of the etioplasts' saponin but with reduced protein and pigment. In the same experiments the enzyme NADPH: protochlorophyllide oxidoreductase showed the same distribution pattern as the CF1-ATPase suggesting its location on the prothylakoids.

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Year:  1981        PMID: 6456902     DOI: 10.1111/j.1432-1033.1981.tb06409.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  7 in total

1.  Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development.

Authors:  Lisa A Blomqvist; Margareta Ryberg; Christer Sundqvist
Journal:  Photosynth Res       Date:  2007-12-11       Impact factor: 3.573

2.  Regulation of photosynthesis by reversible phosphorylation of the light-harvesting chlorophyll a/b protein.

Authors:  J Bennett
Journal:  Biochem J       Date:  1983-04-15       Impact factor: 3.857

3.  Prolamellar body and saponins: Avenacosides are not constituents of Avena etioplasts.

Authors:  S Murakami; M Miyao; M Ikeuchi
Journal:  Plant Cell Rep       Date:  1983-06       Impact factor: 4.570

4.  Reaggregation of etioplast lipids and the formation of prolamellar bodies and thylakoids: An ultrastructural study.

Authors:  H Tönissen; C Lütz
Journal:  Plant Cell Rep       Date:  1984-06       Impact factor: 4.570

Review 5.  Organization of chlorophyll biosynthesis and insertion of chlorophyll into the chlorophyll-binding proteins in chloroplasts.

Authors:  Peng Wang; Bernhard Grimm
Journal:  Photosynth Res       Date:  2015-05-09       Impact factor: 3.573

6.  Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) : I. Localization by immunoblotting in isolated plastids and total leaf extracts.

Authors:  K Dehesh; M Klaas; I Häuser; K Apel
Journal:  Planta       Date:  1986-10       Impact factor: 4.116

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

Authors:  K Dehesh; M Ryberg
Journal:  Planta       Date:  1985-06       Impact factor: 4.116

  7 in total

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