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'ß Carotene' in keywords
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1994 (2)
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1Author    M. Athias, O. Senge, H. Äkon, Hope, KevinM. SmithRequires cookie*
 Title    Structure and Conformation of Photosynthetic Pigments and Related Compounds 3. Crystal Structure of ß-Carotene  
 Abstract    The crystal structure o f the title compound (C40H 56, M w = 536.8) has been redetermined by X-ray diffraction methods in order to achieve a structure at higher resolu­ tion suitable for theoretical calculations. The crystal sys­ tem is monoclinic, P2 ,/«, a = 7.656(2), b = 9.445(5), c -23.536(15) Ä , ß = 93.41(2)°, V = 1698.8(15) Ä 3, Z = 2, D = 1.050 m g/m 3, 130 K. R = 0.071, R w = 0.076. 
  Reference    Z. Naturforsch. 47c, 474 (1992); received June 4 1991/February 24 1992 
  Published    1992 
  Keywords    Crystal Structure, ß-Carotene, Carotenoids, Photosynthesis 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0474_n.pdf 
 Identifier    ZNC-1992-47c-0474_n 
 Volume    47 
2Author    A. M. Akewicz, A. R. Adunz, G. H. SchmidRequires cookie*
 Title    Immunological Evidence for the Binding of ß-Carotene and Xanthophylls onto Peptides of Photosystem I from Nicotiana tabacum  
 Abstract    Photosystem I preparations were obtained from wild type tobacco Nicotiana tabacum var. John William's Broadleaf (JWB) and from the two chlorophyll-deficient mutants N tabacum Su/su and N. tabacum Su/su var. Aurea. The preparations were characterized with respect to the chlorophyll a/b ratio, their photosynthetic activity and their absorption spectroscopic properties. Peptides from these preparations were analyzed by SDS polyacrylamide gel elec­ trophoresis and transferred for the detection of bound carotenoids according to the Western blot procedure to nitrocellulose or Immobilon membranes. The PS I preparation from the wild type JW B consisted of the core and the LH CP complex. The core complex contains the two core peptides with the same apparent MW of 6 6 kD a and several peptides with the lesser molecular masses of 22, 20, 19, 17, 16, 10 and 9 kDa. The light-harvesting protein complex consists of 4 subunits with the molecular masses 28, 26, 25 and 24 kDa. The PS I preparations of the yellow-green mutant Su/su and of the A urea mutant Su/su var. Aurea contain as impurity traces of the Dl and D 2 core peptides of photosystem II and also traces of the chlorophyll-binding photosystem II peptides with the molecular masses 42 and 47 kDa. The peptides of the photosystem I preparation were characterized by specific photosys­ tem I antisera: An antiserum to the photosystem I complex reacts in the Western blot only with the homologous peptides of photosystem I. In comparative analyses with photosystem II preparations this antiserum (directed to photosystem I) reacts, as expected, only with the peptides of the light-harvesting complex. An antiserum to the C P I core peptides reacts only with the 6 6 kD a peptides of photosystem I and gives no cross reaction with heterodimer forms of the D !/D 2 core peptides of photosystem II. In the Western blot procedure by means of polyclonal monospecific antisera to carotenoids it was dem onstrated that ß-carotene is bound in high concentration onto the core peptides CPI and to a lesser extent onto the two larger subunits of the LHCP complex, exhibiting the molecular masses of 28 and 26 kDa. N eoxanthin is bound onto the same peptides. In contrast to this, lutein was only identified on the core peptides C P I and violaxanthin only on the larger subunits of the LH CP complex. As the carotenoids are labelled with antibodies, even after SDS treatm ent in the electrophoresis, it is assumed, that the carotenoids are co­ valently bound via the ionon ring to the respective peptide. 
  Reference    Z. Naturforsch. 49c, 427—438 (1994); received February 17 1994 
  Published    1994 
  Keywords    Photosystem I, ß-Carotene, Lutein, Violaxanthin, Neoxanthin, Antibodies 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0427.pdf 
 Identifier    ZNC-1994-49c-0427 
 Volume    49 
3Author    Shan-Yuan Yang, S. S. BrodyRequires cookie*
 Title    Effect of ß-Carotene on Delayed Light Emission from Aggregated Chlorophyll  
 Abstract    Delayed light emission (DLE) from aggregated chlorophyll is used to probe energy transfer between aggre­ gated chlorophyll and ß-carotene. Preilluminated ß-carotene when injected into a dark chamber containing aggregated chlorophyll, induces DLE from aggregated chlorophyll. If the dark chamber contains only monomeric chlorophyll, there is no DLE. The intensity of DLE is de­ pendent on the time of illumination of ß-carotene. The decay of energy stored by the carotene is not a first order process. The first half life is about 2 min, the next about 1 0 min. 
  Reference    Z. Naturforsch. 45c, 132—134 (1990); received February 6 /August 15 1989 
  Published    1990 
  Keywords    ß-Carotene, Delayed Light Emission, Chlorophyll Aggre­ gates, Fluorescence, Phosphorescence 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0132_n.pdf 
 Identifier    ZNC-1990-45c-0132_n 
 Volume    45 
4Author    O. Kruse, A. Radunz, G. H. SchmidRequires cookie*
 Title    Phosphatidylglycerol and ß-Carotene Bound onto the D 1-Core Peptide of Photosystem II in the Filamentous Cyanobacterium Oscillatoria chalybea  
 Abstract    -particles from the cyanobacterium Oscillatoria chalybea were isolated by fractionating centrifugation. Purification of these particles was achieved by a 22 hours cen­ trifugation over a linear sucrose density gradient at 217.500 X g. The obtained particle frac­ tion exhibited an oxygen evolution activity which corresponded to three times the rate of intact cells and to five times the rate of intact thylakoids. The chlorophyll protein ratio was 1:10 and the ratio manganese/chlorophyll 1:34. SDS-polyacrylamide gel electrophoresis showed that the photosystem Il-fraction is com­ posed of the core peptides D 1 and D2, the chlorophyll-binding peptides CP 43 and CP 47, the extrinsic 33 kDa peptide (manganese stabilizing peptide, MSP) and phycobiliproteins with molecular masses between 16 to 20 kDa. Cyt b559 was not detected in our gel electro­ phoresis assay. Part of the peptides of the 30 kDa-region (D 1, D 2, MSP) occurred as aggre­ gates with a molecular mass of 60 to 66 kDa. The D 1-peptide was isolated from the PS Il-preparation by SDS-gel electrophoresis. The intrinisic peptide reacts in the Western blot procedure with the antiserum to phosphatidyl­ glycerol and with the antiserum to ß-carotene. Incubation of the peptide with the antisera to monogalactosyldiglyceride, sulfoquinovosyldiglyceride and zeaxanthine resulted negatively. The binding of phosphatidylglycerol onto the D 1-peptide was confirmed by lipid analysis in HPLC and fatty acid analysis by gas chromatography. Only this lipid, respectively the typi­ cal fatty acid mixture of this lipid was detected. The lipid is characterized by the fact that the hexadecenoic acid does not exhibit rraws-configuration, as is true for phosphatidylglycerol of higher plants and algae, but occurs in cw-configuration. With the antibody being directed towards the glycerol-phosphate residue and not towards the fatty acids, it can be concluded from the reaction of the antibodies with the bound lipid that the lipid is bound to the peptide via the fatty acid. The negatively charged phosphatidyl­ glycerol increases the hydrophobicity of the peptide and leads to a negatively charged sur­ face favouring binding of cations like calcium and magnesium. The fact that incubation of this PS Il-fraction with phospholipase inhibits photosynthetic activity by 25% which can be fully restored by addition of phosphatidylglycerol, shows that bound phosphatidylglycerol has a functional role. 
  Reference    Z. Naturforsch. 49c, 115—124 (1994); received July 16/October 181993 
  Published    1994 
  Keywords    D 1-Peptide, Phosphatidylglycerol, ß-Carotene, Antibody, Lipid-Protein Binding, Cyanobacterium, Manganese Stabilizing Peptide Photosystem II 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0115.pdf 
 Identifier    ZNC-1994-49c-0115 
 Volume    49