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1Author    Paul Hansmann, Peter SitteRequires cookie*
 Title    Comparison of the Polypeptide Complement of Different Plastid Types and Mitochondria of Narcissus pseudonarcissus  
 Abstract    The protein complement of chloroplasts, prochromoplasts, chromoplasts, and mitochondria of the daffodil (Narcissus pseudonarcissus) has been investigated comparatively by gel electro­ phoresis. Mitochondria do not share common proteins with plastids. On the other hand, there is a broad overlap of the protein complement of the three plastid types investigated, in spite of their different fine structures. There are, however, remarkable differences regarding the relative amounts of many protein species, and certain plastid proteins are entirely absent either from the chloroplasts (e.g., 2 chromoplast proteins in the 60 kDa range) or the chromoplasts (e.g., LHCP). The protein complement of prochromoplasts, which contain chlorophylls and the LHCP, is nevertheless quite more similar to the protein pattern of the chromoplasts than to the one of the chloroplasts. 
  Reference    Z. Naturforsch. 39c, 758—766 (1984); received May 9 1984 
  Published    1984 
  Keywords    Narcissus, Plastids, Mitochondria, Protein Complement, SDS-PAGE 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0758.pdf 
 Identifier    ZNC-1984-39c-0758 
 Volume    39 
2Author    M. Anfred Liitzow, Peter Beyer, Hans KleinigRequires cookie*
 Title    The Herbicide Command Does Not Inhibit the Prenyl Diphosphate-Forming Enzymes in Plastids  
 Abstract    The herbicide Comm and (2-(2-chlorophenyl)m ethyl-4,4-dim ethyl-3-isoxazolidinone) does not affect the in vitro activities o f the plastid enzymes catalyzing the steps leading from isopen­ tenyl diphosphate to geranylgeranyl diphosphate and phytoene, i.e. the isopentenyl diphos­ phate isomerase, prenyl transferase and phytoene synthase. The extractable activities o f these enzymes in herbicide-treated seedlings are also not affected. Nevertheless, the synthesis o f chlorophylls and carotenoids in treated seedlings is severely inhibited in vivo. The mode o f action o f Comm and remains still unknown. 
  Reference    Z. Naturforsch. 45c, 856 (1990); received April 6 1990 
  Published    1990 
  Keywords    Command, Bleaching Herbicide, Prenyl Diphosphates, Carotinoid Formation, Plastids 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0856.pdf 
 Identifier    ZNC-1990-45c-0856 
 Volume    45 
3Author    Jasmina Muraja-Ljubičić, Mercedes Wrischer, Nikola LjubešićRequires cookie*
 Title    Influence of the Herbicides Amitrole and Norflurazon on Greening of Illuminated Potato Microtubers  
 Abstract    Potato microtubers turn green within a few days when kept in the light. The initial phases in this process were observed as early as 12 hours after the onset of illumination. The changes included a pronounced increase in chlorophyll and carotenoid concentrations, accompanied by changes in the protein pattern and in the transformation of amyloplasts and leucoplasts to chloroplasts. The bleaching herbicides amitrole and norflurazon inhibited the synthesis of carotenoids in the illuminated potato microtubers. However, amitrole only delayed greening and an increase in chlorophyll and carotenoid levels became visible as late as four days after the onset of illumination, and the LHC II protein of the photosynthetic membrane was not detected before the seventh day of light exposure. Norflurazon, in contrast, acted as a stronger inhibitor, and microtuber tissues stayed yellowish throughout the experiment. The concentrations of both carotenoids and chlorophylls were very low in tissues treated with this herbicide. The LHC II protein could not be detected after a seven-day light exposure and the plastids were damaged, small in size, without normal thylakoids and with numer­ ous plastoglobules. 
  Reference    Z. Naturforsch. 54c, 333 (1999); received November 30 1998/January 21 1999 
  Published    1999 
  Keywords    Solanum tuberosum L cv Istra, Microtuber, Plastid, Amitrole, Norflurazon 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0333.pdf 
 Identifier    ZNC-1999-54c-0333 
 Volume    54 
4Author    ThomasBarbara Kirsch, Helmut Rojahn, KindiRequires cookie*
 Title    Diphosphatase Related to Lipid Metabolism and Gluconeogenesis in Cucumber Cotyledons: Localization in Plasma Membrane and Etioplasts but not in Glyoxysomes  
 Abstract    Diphosphatase (inorganic pyrophosphatase) activity was localized within compartments of cotyledons of germinating cucumber seeds during the stage of maximal conversion of fat into carbohydrates. At this stage, almost 2 mol pyrophosphate are produced during the formation of one mole sucrose from 0.28 mol triglyceride. When organelles of the 2000 x g pellet or 10,000 x g pellet were separated by density gradient centrifugation and gradient flotation, the diphosphatase activity paralleled the profiles of markers of the plastid stroma but was virtually absent from the glyoxysomes. Within the fraction of small vesicles and membranes, diphosphatase was attributed to the plasma membrane. The main portion of diphosphatase, contained in the plastids, was partially purified by chromatography on anion exchange resin and molecular sieving, leading to a 75-fold enrichment compared to the stroma fraction. Trace amounts of diphosphatase observed in the glyoxysomal fraction were analyzed in the same way. Comparison of the isoelectric points and the activity profile at different pH values and the inhibitory effect of the various cations indicated that the trace amounts of diphosphatase activity in the glyoxysome fraction represented contaminations originating from the plastids. The plasma membrane form of diphosphatase is an integral membrane protein which was solubilized with octylglucoside. It was shown to differ from the plastid form in pH optimum and sensitivity towards bivalent cations. All forms of diphosphatase were clearly distinguished from other phosphohydrolytic activities. 
  Reference    Z. Naturforsch. 44c, 937 (1989); received June 7/July 25 1989 
  Published    1989 
  Keywords    Plastid, Plasma Membrane, Glyoxysome, Diphosphatase (Pyrophosphatase), Cucumber Mobilization 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0937.pdf 
 Identifier    ZNC-1989-44c-0937 
 Volume    44