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1Author    Cornelius Lütz, Jürgen Benz, Wolfhart RüdigerRequires cookie*
 Title    Esterification of Chlorophyllide in Prolamellar Body (PLB) and Prothylakoid (PT) Fractions from ^4 vena sativa Etioplasts  
 Abstract    Etioplast membranes were fractionated into enriched prothylakoid (PT) and prolamellar body fraction (PLB) by known procedures [2]. The photoconversion o f Protochlide to Chlide was 77% in the PT fraction but only 65% in the PLB fraction with optimum NADPH concentrations. The subsequent esterification reaction proceeds in both fractions indicating that the enzyme chlorophyll synthetase is present in both fractions. In the PLB fraction, 10-15% more Chip is formed than in the PT fraction. It is concluded that the concentration of the endogenous phytol precursor is higher in the membranes still present in the PLB fraction than in the PT fraction. 
  Reference    Z. Naturforsch. 36c, 58—6 (1981); received October 24 1980 
  Published    1981 
  Keywords    Prolamellar Bodies, Thylakoids, Chlorophylls 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0058.pdf 
 Identifier    ZNC-1981-36c-0058 
 Volume    36 
2Author    CarlosS. Andreo, ElenaG. Orellano, HermannM. NiemeyerRequires cookie*
 Title    Uncoupling of Spinach Thylakoids by Gramine  
 Abstract    The indol alkaloid gramine inhibited photophosphorylation, Pi-ATP exchange reaction and proton gradient, and enhanced electron transport in spinach thylakoids with I 50 around 0.2 m M . It thus behaves as a typical uncoupler of photophosphorylation. 
  Reference    Z. Naturforsch. 39c, 746—748 (1984); received March 19 1984 
  Published    1984 
  Keywords    Gramine, Indol Alkaloids, Thylakoids, Uncoupler 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0746.pdf 
 Identifier    ZNC-1984-39c-0746 
 Volume    39 
3Author    A.-KJ. Sallal, N. A. NimerRequires cookie*
 Title    The Presence of Malate Dehydrogenase in Thylakoids of Anabaena cylindrical Nostoc muscorum and Chlorogloeopsis fritschii  
 Abstract    The location o f malate dehydrogenase in the cyanobacteria, Anabaena cylindrica, Nostoc muscorum and Chlorogloeopsis fritsch ii was investigated by the fractionation o f cell-free ex­ tracts. The bulk o f the enzyme activity was associated with the thylakoid membrane fraction, which also exhibited complete photosynthetic electron transport reactions. Malate dehydro­ genase activity and photosystem II activities were inhibited by hom ologous antisera raised against isolated thylakoid membranes. 
  Reference    Z. Naturforsch. 45c, 249 (1990); received July 4/O ctober 13 1989 
  Published    1990 
  Keywords    Cyanobacteria, Malate Dehydrogenase, Thylakoids 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0249.pdf 
 Identifier    ZNC-1990-45c-0249 
 Volume    45 
4Author    G. Uhlenbruck, A. RadunzRequires cookie*
 Title    Use of Heterophilic Agglutinins in Plant Serology  
 Abstract    In previous communications it has been demonstrat-ed that monogalactosyl diglyceride and the anionic chloroplasts lipids can be detected on the thylakoid membrane by specific antisera 1_3 . The antigen deter-minants are of carbohydrate nature as was shown by specific agglutination inhibition tests. They are located on the outer surface of the thylakoid membrane and are directly accessible to the antibodies. The latter has been proven for the monogalactolipid 1 , whereas the de-terminants having the carbohydrate structure like that of sulphoquinovosyl diglyceride 2 stick out of the sur-face like phosphatidyl glycerol too 3 , but are topogra-phically rather arranged in gaps or pores of the membrane. Fatty acids are not involved in this antigen-antibody reactions as precipitation studies with hydrat-ed lipids and with lipids of different fatty acid com-positions have revealed. On the other side, if sugar components represent the immunologically determinant groups, then it should be possible to confirm the results obtained with vertebrate antisera by using heterophilic agglutinins from plants (so-called lectins) 4 , inverte-brates and fish eggs. These are known to be excellent tools for the specific detection of terminal and inner-chain carbohydrate structures of different configurations and conformations 5 . As D-galactose is the main deter-minant sugar in plant glycolipids, we tested some of the galactose specific lectins in our system. It could be found, that the agglutinin from Ricinus communis, the anti-galactosyl specificity of which is well established 4 , agglu-tinated chloroplasts and thylakoidfragments in a very specific way. This agglutination was inhibited by 0.03 M D-galactose, 0.06 M lactose, raffinose, stachyose, mono-galactosyl glycerol (/9-glycosidic linkage), and digalac-tosyl glycerol (a-glycosidic linkage of D-galactose), but not by D-glucose, and L-arabinose. In addition, the spe-cific anti-a-galactosyl agglutinin 6 ("anti-B") from Salmo trutta (trout) also reacts well, especially after protease treatment. It is inhibited by carbohydrates with terminal a-glycosidic bound D-galactose (raffinose, stachyose, digalactosyl glycerol 0.03 M) and not by monogalactosyl glycerol, lactose, D-glucose, D-and L-arabinose. We got weaker reactions with agglutinins from fungal origin like Fomes fomentarius, a lectin known as anti-B (a-galactosyl) reagent 4 ' 7 , whereas other agglutinins (Arachis hypogoea "anti-T") directed to D-galactose-like structures 8 gave very weak 
  Reference    (Z. Naturforsch. 27b, 1113 [1972]; received June 27 1972) 
  Published    1972 
  Keywords    Heterophilic agglutinins, glycolipids, chloroplasts, thylakoids, lectins 
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 TEI-XML for    default:Reihe_B/27/ZNB-1972-27b-1113_n.pdf 
 Identifier    ZNB-1972-27b-1113_n 
 Volume    27 
5Author    Govindjee, Paul Mathis, Claudie Vem Otte, Daniel Wong, Satham Saphon, ThomasW. Ydrzynskic, Jean-M Arie BriantaisRequires cookie*
 Title    Cation Effects on System II Reactions in Thylakoids: Measurements on Oxygen Evolution, the Electrochromic Change at 515 Nanometers, the Primary Acceptor and the Primary Donor  
 Abstract    Divalent cations are known to decrease the "spillover" of excitation energy from photosystem II (PS II) to PS I. At low light intensities, this does lead to an increased quantum yield of photo­ reactions in PS II. Contrary to some suggestions that PS II is activated at high light intensities, or in strong flashes of light by the addition of Mg2+, we suggest here that Mg2+ ions may not activate reaction center II, P 680. After brief light flashes, we do not find any significant enhancement in (a) 0 2 yield/flash, (b) proton yield/flash, (c) the amplitude of charge separation in PS II, as moni­ tored by 515 nm absorbance change, and (d) the amplitude of the reduced primary acceptor, as monitored by 320 nm absorbance change. Data on absorbance change at 820 nm suggest that the absence of Mg2+ does not lead to inactivation of electron donation to P 680+. 
  Reference    Z. Naturforsch. 34c, 826—830 (1979); received July 9 1979 
  Published    1979 
  Keywords    Photosynthesis, Flash Yields, Cation Effects, Photosystem II, Thylakoids 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0826.pdf 
 Identifier    ZNC-1979-34c-0826 
 Volume    34 
6Author    Henrik Laasch, Klaus Pfister, Wolfgang UrbachRequires cookie*
 Title    Comparative Binding of Photosystem II — Herbicides to Isolated Thylakoid Membranes and Intact Green Algae  
 Abstract    The binding of the photosystem II herbicides diuron (DCM U), atrazine (s-triazine), ioxynil and dinoseb (substituted phenols) to isolated spinach thylakoids was saturated in less than 2 min in the dark. In intact cells of the green alga Ankistrodesmus b. it took 10 to 20 min to reach the binding equilibrium. Binding affinity of diuron, atrazine, dinoseb, measured as equilibrium binding constants, was found to be comparable in isolated thylakoids and intact algal cells. For ioxynil, reduced binding affinity was observed in algae. The concentration of binding sites in thylakoids and intact cells was determined to be 300-500 chl/inhibitor binding site, suggesting a 1:1 stoichiometry between bound herbicide and electron transport chains. In intact cells only the phenol herbicides ioxynil and dinoseb showed increased concentrations of binding sites. Strong correlation of herbicide binding and inhibition o f electron transport was found for diuron in isolated thylakoids and intact cells. In thylakoids this is valid also for atrazine and dinoseb. For ioxynil a difference between the amount of binding and inhibition was found. This correlation o f herbicide binding and inhibition proves that binding specifically occurs at the inhibition site at photosystem H. In addition to the specific binding, for all four herbicides studied, (except for ioxynil in thylakoids) unspecific binding was observed in thylakoids as well as in algae, which was not related to inhibition. 
  Reference    Z. Naturforsch. 36c, 1041—1049 (1981); received July 13 1981 
  Published    1981 
  Keywords    Herbicides, Herbicide Binding, Photosynthesis, Thylakoids, Algae 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-1041.pdf 
 Identifier    ZNC-1981-36c-1041 
 Volume    36 
7Author    K.H G Rum BachRequires cookie*
 Title    Distribution of Chlorophylls, Carotenoids and Quinones in Chloroplasts of Higher Plants  
 Abstract    Leaves, cotyledons, isolated chloroplasts and subplastid fractions (thylakoids and envelopes) o f radish (Raphanus sativus L. cv. Saxa) and spinach (Spinacia oleracea L. cv. M atador) were assayed for their pigment and quinone content and com position. Virtually all the chlorophylls, carotenoids and quinones were contained in the thylakoids. Envelopes prepared by the method described contained very low amounts o f chlorophyll a and b, violaxanthin and neoxanthin, but no /7-carotene, lutein, zeaxanthin and antheraxanthin. Am ong the quinones trace am ounts o f plastoquinone and a-tocopherol but no plastohydroquinone, a-tocoquinone and phylloquinone were detected. Presented data may be taken as evidence that in vivo the chloroplast envelope is not a location site o f carotenoids and quinones as generally accepted. Possible im plications for the biosyntheses o f quinones and pigments are discussed. 
  Reference    Z. Naturforsch. 38c, 996—1002 (1983); received August 16 1983 
  Published    1983 
  Keywords    Carotenoids, Chlorophylls, Chloroplasts, Envelopes, Quinones, Thylakoids 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0996.pdf 
 Identifier    ZNC-1983-38c-0996 
 Volume    38 
8Author    S. J. Coughlan, U. SchreiberRequires cookie*
 Title    Light Induced Changes in the Conformation of Spinach Thylakoid Membranes as Monitored by 90° and 180° Scattering Changes: A Comparative Investigation  
 Abstract    A series o f investigations on light induced thylakoid m em brane conform ational changes has been carried out using scattering changes m easured either at 9 0 ° or 180° (transm ittance changes) as criteria for changes in membrane structure upon illum ination. T hese two phenom ena were found to react similarly to a range o f photosynthetic inhibitors, to changes in the ionic (M g2+, H +) concentration, and to have similar difference spectra. H owever, it was found possible to distinguish these two phenomena by the differences in the kinetics o f the light induced rise times. This could be shown most clearly using an A m inco D W 2 spectrophotom eter with the measuring beam deflected through 90° by front face mirrors. The dark decay tim e o f the two scattering changes was similar. These results are discussed in relation to the hypothesis that the light induced narrow angle 90° scattering response represents m icroconform ational m em brane changes in response to proton uptake, and the 180° scattering changes represent a m ixed response including changes in the stacking o f thylakoids. 
  Reference    Z. Naturforsch. 39c, 1120—1127 (1984); received August 6 1984 
  Published    1984 
  Keywords    Conformational Changes, Thylakoids, Scattering Changes, C om parison 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1120.pdf 
 Identifier    ZNC-1984-39c-1120 
 Volume    39 
9Author    M. Agdolna, D. Roppa, JiriM. Asojidek, G. Á. Bor, H. Orváth, M. Droppa, M. L. Ghirardi, G. Horvath, A. Melis, Biochim Biophys, ActaRequires cookie*
 Title    Changes of the Polypeptide Composition in Thylakoid Membranes during Differentiation  
 Abstract    Changes in membrane polypeptide com position during greening o f etiolated maize were in­ vestigated to confirm the existence o f the developm ental polypeptides o f 1 2 -15 kDa described recently in virescent soybean mutant []. These low molecular weight polypeptides were the most abundant proteins at the early stage o f greening, but were largely absent from fully developed thylakoids. During greening the relative concentration o f the 1 2 -1 5 kDa polypep­ tides were inversely proportional to that o f LHC II, suggesting a role o f these polypeptides in the assembly o f the LHC II and/or chloroplast developm ent. 
  Reference    Z. Naturforsch. 45c, 253—145 (1990); received October 13 1989/January 2 1990 
  Published    1990 
  Keywords    Chloroplasts, Greening, Membrane Proteins, Photosynthesis, Thylakoids 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0253.pdf 
 Identifier    ZNC-1990-45c-0253 
 Volume    45 
10Author    W. S. Cohen, J. R. BartonRequires cookie*
 Title    The Use of 0 2-Evolving Subchloroplast Particles to Study Acceptor and Inhibitor Sites on the Reducing Side of Photosystem II  
 Abstract    Photosystem II particles that retain the ability to evolve 0 2 have been used to exam ine acceptor and inhibitor sites in the photosynthetic electron transfer chain between Q and plasto-quinone. Employing the water to dichlorobenzoquinone reaction to assay photosystem II activity, we have demonstrated that electron transport in thylakoids and particles is equally sensitive to inhibition by D C M U , dinoseb, metribuzin, H Q N O and DBMIB. Based on differential sensitivity to inhibition by D C M U vs. H Q N O or DBMIB, we suggest that when synthetic quinones, e.g. 2,6-dichlorobenzoquinone operate as Hill reagents in particles they are reduced primarily by the plastoquinone pool. W hen synthetic quinones, e.g. 5,6-m ethylenedioxy-2,3-dim ethyl benzoquinone act as autoxidizable acceptors they accept electron from the Q /B com plex at a point that is located between the D C M U and H Q N O (DBM IB) inhibition sites. 
  Reference    Z. Naturforsch. 38c, 793—798 (1983); received April 26 1983 
  Published    1983 
  Keywords    Thylakoids, Photosystem II Particles, Q uinones, Inhibitors, Electron Transfer 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0793.pdf 
 Identifier    ZNC-1983-38c-0793 
 Volume    38 
11Author    W. LöffelhardtRequires cookie*
 Title    The Biosynthesis of Phenylacetic Acids in the Blue-Green Alga Anacystis nidulans: Evidence for the Involvement of a Thylakoid-Bound L-Amino Acid Oxidase  
 Abstract    Phenylacetic acid and p-hydroxyphenylacetic acid are formed upon incubation of photosynthetic membranes from the prokaryotic alga Anacystis nidulans with L-phenylalanine and L-tyrosine, respectively. The corresponding phenylpyruvic acids act as intermediates as shown by trapping them as the stable oximino acids. The first step in this reaction sequence appears to be catalyzed by a thylakoid-bound L-amino acid oxidase. Already existing evidence concerning phenylacetic acid formation at thylakoid membranes of higher plants via an L-amino acid oxidase and the results obtained with A. nidulans give another example of aromatic amino acids between chloroplasts and 
  Reference    (Z. Naturforsch. 32c, 345—350 [1977]; received February 14 1977) 
  Published    1977 
  Keywords    Membrane-Bound Enzymes, Anacystis nidulans, Thylakoids, Phenylacetic Acids, L-Amino Acid Oxidase 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0345.pdf 
 Identifier    ZNC-1977-32c-0345 
 Volume    32 
12Author    Hans-Joachim Soli, Ellen OlschewskiRequires cookie*
 Title    Photoaffinity Labeling o f Spinach Thylakoids and Cytochrome ^  
 Abstract    /-C o m p le x by the Hydrophobic Reagent 3-(Trifluorom ethyl)-3-(/n-[125I]iodophenyl)-diazirine W alter O ettm eier, In isolated spinach thylakoids the hydrophobic photo­ reactive probe 3-(trifluoromethyl)-3-(m-[I25I]iodophenyl-diazirine almost exclusively labels the photosystem I reac­ tion center and the light-harvesting chlorophyll alb protein. In isolated cytochrome b6//-complex, all four components of the complex get labeled, but to a different extent. The amount of labeling in the protein components is correlated to the number of polypeptide segments embedded in the membrane system. 
  Reference    Z. Naturforsch. 40c, 454 (1985); received February 25 1985 
  Published    1985 
  Keywords    Photoaffinity Label, Carbene Reagent, Spinach Thylakoids, Cytochrome b j f -complex, Membrane Proteins 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0454_n.pdf 
 Identifier    ZNC-1985-40c-0454_n 
 Volume    40 
13Author    S. C. Sabat, V. Vijayavergiya, B. C. Tripathy, PrasannaM. OhantyRequires cookie*
 Title    Inhibitory Effect of Crown Compound on Photoelectron Transport Activity of Beet Spinach Thylakoid Membranes  
 Abstract    The effect o f K-picrate-18-crown-6 (crown) on the photoelectron transport activity o f beet spinach thylakoid membranes was investigated. A ddition o f micromolar concentration o f crown to thylakoid preparation inhibited p-benzoquinone, chloride-indophenol, methyl violo-gen supported Hill activities maximally by 75 per cent in a concentration dependent manner. However, the photosystem I catalyzed reaction remained insensitive to crown suggesting that crown specifically inhibits photosystem II electron transport. Addition o f exogenous electron donors like hydroxylamine or diphenylcarbazide failed to restore the crown induced inhibition o f photosystem II electron transport and lowering o f steady state chlorophyll a fluorescence yield. These observations suggest that crown also inhibits photosystem II catalyzed electron transport after the donation sites o f these exogenous donors. Washing o f the crown pre-treat-ed thylakoids with isolation buffer, relieved the crown inhibited electron transport activity, indicating that this inhibition is reversible. Furthermore, in hydroxylamine washed thylakoids which are devoid o f 0 2 evolution capacity, the hydroxylamine induced increase in chlorophyll a fluorescence o f variable yield was quenched by the addition o f crown. These observations suggest that crown affects the oxygen evolution and inhibits at a site close to photosystem II reaction centres. 
  Reference    Z. Naturforsch. 46c, 87 (1991); received August 14 1990 
  Published    1991 
  Keywords    Crown-Ether, Electron Transport, Photosystem II, Thylakoids, Beet Spinach ( Beta vulgaris) 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0087.pdf 
 Identifier    ZNC-1991-46c-0087 
 Volume    46