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'Bile Pigments' in keywords Facet   section ZfN Section C  [X]
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1982 (1)
1980 (1)
1977 (1)
1Author    Hugo Scheer, W. Erner KuferRequires cookie*
 Title    Conformational Studies on C-Phycocyanin from Spirulina platensis  
 Abstract    The chromophore-protein interactions of C-phycocyanin (C-PC) from Spirulina platensis have been studied by following the partial and complete denaturation with UV-Vis spectroscopy. From comparison with published MO calculations, an elongated conformation of the chromophore is sug­ gested for native C-PC, a cyclic one for denatured C-PC. By means of partial denaturation, a step­ wise unfolding of the protein has been demonstrated. The presence of at least two sets of spectro­ scopically different diromophores is suggested from the partial denaturation and low temperature experiments. 
  Reference    (Z. Naturforsch. 32c, 513 [1977]; received April 25 1977) 
  Published    1977 
  Keywords    Bile Pigments, Protein Interaction, Conformation, Denaturation 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0513.pdf 
 Identifier    ZNC-1977-32c-0513 
 Volume    32 
2Author    W. Olfhart Rüdiger, Thom As Brandlmeier, Inge Bios, Jens-Peter Gossauer, WellerRequires cookie*
 Title    Isolation of the Phytochrome Chromophore. The Cleavage Reaction with Hydrogen Bromide A lbert  
 Abstract    The cleavage o f the bilin chromophore from C-phycocyanin with hydrogen bromide yields 3E-configurated phycocyanobilin (4) as the major and 3 Z-configurated phycocyanobilin (5) as the minor reaction product. The reaction o f synthetic 3E-configurated phytochromobilin (2) with hydrogen bromide and methanol leads only to a methanol adduct at the C-18 side chain (7) whereas the same reaction with the 3Z-configurated phytochromobilin (3) leads to 7 and 2. The bilin chromophore was cleaved also from phytochrome after preparation o f phytochromobilin peptides. The detection o f 2 and 7 suggested that 3Z-and 3E-configurated phytochromobilin were the primary products o f cleavage from phytochrome. A reaction scheme is given which can explain the results o f the reaction with hydrogen bromide and methanol. 
  Reference    Z. Naturforsch. 35c, 763—769 (1980); received July 11 1980 
  Published    1980 
  Keywords    Phytochrome, Bile Pigments, Phytochromobilin, Thioether Cleavage, C-Phycocyanin 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0763.pdf 
 Identifier    ZNC-1980-35c-0763 
 Volume    35 
3Author    W. Küfer, H. ScheerRequires cookie*
 Title    Rubins and Rubinoid Addition Products from Phycocyanin  
 Abstract    The verdin-type Chromophore o f denatured C-phycocyanin (1) from Spirulina platensis is reduced to the corresponding rubin (2 a) by sodium borohydride. The structure assigned is in agreement with the uv-vis spectroscopic properties of the product and was deduced from model studies with free bile pigments. Analogous model studies using sodium dithionite demonstrated a two-fold reactivity for this reagent, leading to products which are both o f the rubin spectral type under the conditions tested. True rubins (10,22-dihydrobilindions) are formed in low yield only if an excess o f reagent is used in methanol/water mixtures. It is accompanied by polar addition product(s) o f the same spectral type, which are generally formed exclusively. In particular, no bilirubin was formed under the reaction conditions previously applied for the chemical modification o f phycobiliproteins and phytochrome. From this finding and from the strikingly different properties o f the borohydride and dithionite products, o f phycocyanin upon renaturation, the dithionite product is suggested to be a rubinoid addition product (2 b) rather than a hydrogenation product. In contrast to the dithionite addition product 2 b of phycocyanin, the chromophore o f the true phycorubin (2 a) remains stable upon renaturation. The uv-vis spectral properties of the chromophore are not markedly different whether the apoprotein is in its native or denatured state. The different electrophoretic mobilities o f native (renatured) phycocyanin compared to the renatured borohydride product suggest that these two have different protein conformations. The preparation of these phycorubins renders the extensive techniques o f bilirubin chemistry applicable in the study o f biliproteins. 
  Reference    Z. Naturforsch. 37c, 179—192 (1982); received December 151981 
  Published    1982 
  Keywords    Phycocyanin, Phycorubin, Bile Pigments, Biliverdin, Bilirubin 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0179.pdf 
 Identifier    ZNC-1982-37c-0179 
 Volume    37