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1Author    Friederike Koenig, Wilhelm Menke, Hans Craubner, GeorgH. Schmid, Alfons RadunzRequires cookie*
 Title    Photochemically Active Chlorophyll-Containing Proteins from Chloroplasts and their Localization in the Thylakoid Membrane  
 Abstract    After solubilization of stroma-freed chloroplasts with deoxycholate, the lipids and the detergent used are separated from the proteins by gel filtration. In this way not denatured pigment-con-taining protein preparations were obtained. The particles in fraction 1 exhibited a molecular weight of 600 000 and contained an average of 25 chlorophyll molecules. The circular dichroism spectrum showed exciton splitting of the red band. The particles in fraction 2 contained 1 chloro-phyll molecule and exhibited a molecular weight of 110 000. The particles in fraction 3 also contained only 1 chlorophyll molecule and had a molecular weight of between 80 000 and 100 000. Pure preparations of fraction 1 only carried out the methylviologen M e h 1 e r reaction with the dichlorophenol indophenol/ascorbate couple as electron donor. Fraction 3 only reduced ferri-cyanide with diphenylcarbazide as an electron donor in the light. Fraction 2 exhibited both the photosystem I reaction and the photosystem II reaction. An antiserum to extracted fraction 1 does not inhibit electron transport in the intact lamellar system. The photoreduction of methylviologen is only inhibited after disruption of the thylakoids. The antiserum to fraction 2 inhibits the photo-reduction of methylviologen in the intact lamellar system. Consequently, one inhibition site for this photosystem I reaction must be located on the inner and another on the outer surface of the thylakoid membrane. In addition, antibodies to fraction 1 are specifically adsorbed onto the lamellar system without any effect on electron transport and without a concomitant agglutination. Antibodies to fraction 3 partially inhibit the photoreduction of ferricyanide with diphenylcarbazide as an electron donor in the intact lamellar system. Hence, the inhibition site of this system II reaction is located on the outer surface of the thylakoids. We have reason to believe that the inhibition sites not reacting are located in the partitions, which are not accessible to antibodies. 
  Reference    (Z. Naturforsch. 27b, 1225 [1972]; received July 5 1972) 
  Published    1972 
  Keywords    Chloroplasts, membranes, proteins, photosynthesis, antibodies 
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 TEI-XML for    default:Reihe_B/27/ZNB-1972-27b-1225.pdf 
 Identifier    ZNB-1972-27b-1225 
 Volume    27 
2Author    M. KumakuraRequires cookie*
 Title    Association of an Antibody-Conjugated Enzyme with Synthetic Polymers Dissolved in Organic Solvents  
 Abstract    A n antibody of a tumor marker (a-fetoprotein) conju­ gated with peroxidase was dispersed in organic solvents including synthetic polymers, and the interaction o f the antibody with the polymers was investigated. It was found that the antibody-conjugated enzyme is associated with the polymers dissolved in hydrophobic organic sol­ vents. The association correlated with the polym eriza­ tion degree, concentration, and nature of the polymers. 
  Reference    Z. Naturforsch. 49c, 891—8 (1994); received January 10/August 15 1994 
  Published    1994 
  Keywords    Antibody, Enzyme, Association, Polymer, Solvent 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0891_n.pdf 
 Identifier    ZNC-1994-49c-0891_n 
 Volume    49 
3Author    GeorgH. Schmid, Alfons Radunz, Wilhelm MenkeRequires cookie*
 Title    The Effect of an Antiserum to Plastocyanin on Various Chloroplast Preparations  
 Abstract    A monospecific antiserum to tobacco plastocyanin agglutinates strom a-free sw ellable chloroplasts from wild type tobacco, (N ico tia n a tabacum var. John William's Broadleaf) from the tobacco aurea mutant Su/su2, (N ico tia n a tabacum var. Su/su2) from A ntirrh in um m aju s and spinach (Spi-nacia o lera cea). In this condition the antiserum inhibits linear photosynthetic electron flow in tobacco and spinach chloroplasts. This inhibition of electron transport as well as the agglutination are not observed if the chloroplasts have been sonicated prior to antiserum addition. This is due to the fact that plastocyanin is removed by ultrasonication. The antiserum stimulates a number of photophosphorylation reactions in tobacco chloroplasts. This stimulation is always larger in the aurea mutant chloroplasts and in chloroplasts from yellow leaf patches of a variegated tobacco mutant (N . tabacu m , var. N C 95) than in the green type chloroplasts. The stimulation appears to be a consequence of the inhibition of linear electron transport. The antiserum does not affect PMS-mediated cyclic photophosphorylation in tobacco chloroplasts from the wild type whereas the reaction appears stimulated in the tobacco mutant chloroplasts. However, menadione-mediated cyclic photo­ phosphorylation is inhibited upon addition of the antiserum. The same is true for noncyclic photo­ phosphorylation coupled to electron transport in the aerobic system diaminodurene/ascorbate — > methylviologen in the presence of N-tetraphenyl-p-phenylenediamine in spinach chloroplasts. If the lamellar system of A n tirrh in u m and spinach has lost its swellability neither agglutination nor inhibition of electron transport is observed. However, also in this state antibodies to plasto­ cyanin are specifically adsorbed onto the surface of the thylakoid membrane. This state which is characterized by a morphologically well preserved lamellar system is realized in chloroplast prepa­ rations from A n tirrh in um and spinach and is termed stroma-freed, chloroplasts. In both states of the molecular structure of the thylakoid membrane, plastocyanin is located in the outer surface of the thylakoid. However, it cannot be excluded that functioning plastocyanin is also located in the interior of the thylakoid membrane. 
  Reference    (Z. Naturforsch. 30c, 201 [1975]; received December 9 1974) 
  Published    1975 
  Keywords    Photosynthesis, Plastocyanin, Antibodies, Chlorophyll-deficient Tobacco Mutants 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0201.pdf 
 Identifier    ZNC-1975-30c-0201 
 Volume    30 
4Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane I. Maximal Antibody Binding and Adsorption of Antibodies to Lipids  
 Abstract    The binding of antibodies onto the lamellar system of A ntirrhinum m ajus was determined in dependence on the serum addition. The unspecific adsorption of serum proteins was taken into account or eliminated. The binding of antibodies as a function of the amount of serum added is seen from a saturation curve. From an antiserum obtained by hyperimmunization with stroma-freed chloroplasts, the chloroplasts bind maximally 1 gram antibodies per gram stroma-freed chloro­ plasts. From an antiserum to the proteins of the thylakoid membrane prepared in the same way an equal amount of antibodies is adsorbed. It is assumed that with this amount the surface of the lamellar system accessible to antibodies is completely covered by antibodies. For an antiserum to monogalactosyl diglyceride a maximal antibody binding of 0.16 g, for sulphoquinovosyl diglyceride 0.12 g and for phosphatidyl glycerol 0.13 g of antibodies per gram stroma-freed chloroplasts are obtained. The significance of these results with respect to the molecular surface structure of the thylakoid membrane is discussed. 
  Reference    (Z. Naturforsch. 30c, 484—488 [1975]; received April 11975) 
  Published    1975 
  Keywords    Chloroplasts, Lipids, Proteins, Antibodies, Membrane Structure 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0484.pdf 
 Identifier    ZNC-1975-30c-0484 
 Volume    30 
5Author    Alfons RadunzRequires cookie*
 Title    Localization of the Tri-and Digalactosyl Diglyceride in the Thylakoid Membrane with Serological Methods  
 Abstract    Trigalactosyl diglyceride was isolated from leaves of Urtica dioica and characterized by thin layer chromatography, infrared spectroscopy and by its fatty acid composition. An antiserum to the trigalactolipid was obtained by immunization of rabbits. By means of inhibition experiments with oligosaccharides and mono-and digalactosyl glycerol it was demonstrated that the antibodies are directed towards the a-galactosyl-(1 -> 6) -a-galactosyl-(1 — ► 6) -/5-galactosyl-(1 -*■ 1) -glycerol con­ figuration of the trigalactosyl diglyceride. Monogalactosyl diglyceride and sulfoquinovosyl diglyce­ ride do not react with this antiserum. However, a cross reaction was observed with digalactosyl diglyceride. The presence of antibodies to tri-and digalactosyl diglyceride was demonstrated in antisera to different chloroplast preparations of Antirrhinum majus and Spinacia oleracea. The antiserum to the trigalactolipid agglutinates stroma-freed chloroplasts. Membrane fragments obtained by the ultra sonication were precipitated. The antiserum is exhausted by trigalactosyl di­ glyceride but not by digalactosyl diglyceride or digalactosyl glycerol. The antiserum treated with digalactosyl glycerol and digalactosyl diglyceride also agglutinated stroma-freed chloroplasts. 1 g stroma-freed chloroplasts binds 0.17 g antibodies to trigalactolipid. Membrane fragments bind more antibodies to trigalactolipids than stroma-freed chloroplasts. From the agglutination tests it follows that the antigenic determinants of the trigalactolipid and the digalactolipid are localized in the outer surface as well as in the surface directed towards the inside of the thylakoid membrane. 
  Reference    (Z. Naturforsch. 31c, 589 [1976]; received July 19 1976) 
  Published    1976 
  Keywords    Trigalactosyl Diglyceride, Digalactosyl Diglyceride, Antibodies, Chloroplasts, Thylakoid Membrane 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0589.pdf 
 Identifier    ZNC-1976-31c-0589 
 Volume    31 
6Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane II. Distribution of Lipids and Proteins at the Outer Surface of the Thylakoid Membrane  
 Abstract    The number of antibody molecules which stroma-freed chloroplasts can bind out of the mono-specific antisera to monogalactosyl diglyceride, tri-and digalactosyl diglyceride, sulfoquinovosyl diglyceride, phosphatidyl glycerol, sitosterol, plastoquinone, lutein and neoxanthin was determined. This number was compared to the number of antibody molecules which stroma-freed chloroplasts can maximally bind. The result is that the antibodies to the individual lipids cover at most 17 per cent of the accessible thylakoid membrane surface. From a serum which contains both antibodies to the proteins and lipids of the thylakoid mem­ brane, not more antibody molecules are bound than from a serum to the proteins. This means that antibodies to proteins are able to cover up the entire accessible surface of the thylakoids whereas a mixture of antibodies to the lipids, listed above, cover only one forth of the surface. Consequently, antibodies which are bound to proteins can cover up the lipid areas entirely and in turn antibodies which are bound to lipids cover up parts of the protein areas. From this it follows that the portion of the surface, which is made up by lipids must be considerably smaller than 24 per cent. Furthermore, it follows from these experiments that the lipid areas are small and that lipids probably only fill up the gaps between the protein molecules. 
  Reference    (Z. Naturforsch. 32c, 597 [1977]; received May 6 1977) 
  Published    1977 
  Keywords    Chloroplasts, Lipids, Proteins, Antibodies, Membrane Structure 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0597.pdf 
 Identifier    ZNC-1977-32c-0597 
 Volume    32 
7Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane IV. Phosphatides and Xanthophylls in the Outer Surface of the Thylakoid Membrane  
 Abstract    Antisera to the phosphatides phosphatidyl inositol and phosphatidyl choline as w ell as to the xanthophylls violaxanthin and zeaxanthin were obtained by immunization of rabbits. The phosphatidyl choline antiserum did not give cross reactions with thylakoid membrane glycolipids, nor with phosphatidyl glycerol and phosphatidyl inositol. The antiserum to phosphatidyl inositol also did not react with the glycolipids and phosphatidyl choline. However, a cross reaction with phosphatidyl glycerol was observed. Exhaustion tests revealed, that the phosphatidyl inositol antiserum was fully neutralized with the homologous phosphatide, but not with phosphatidyl glycerol. Antibodies to the phosphatides phosphatidyl inositol and phosphatidyl choline react with 
  Reference    Z. Naturforsch. 33c, 941 (1978); received October 2 1978 
  Published    1978 
  Keywords    Phosphatides, Xanthophylls, Chloroplasts, M em bran e Structure, Antibody 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0941.pdf 
 Identifier    ZNC-1978-33c-0941 
 Volume    33 
8Author    Alfons RadunzRequires cookie*
 Title    Binding of Antibodies onto the Thylakoid Membrane. V. Distribution of Proteins and Lipids in the Thylakoid Membrane  
 Abstract    Binding of antibodies to proteins and lipids onto fragments of the thylakoid membrane was stu­ died and compared with the binding o f antibodies by stroma-freed chloroplasts. The mem brane fragments were prepared from strom a-free chloroplasts by ultrasonication and fractional cen­ trifugation. The fragments have an average diam eter of 200 A. T heir thickness corresponds to that of the thylakoid membrane. The m em brane fragments adsorb out o f an antiserum to lipids appro­ ximately the same am ount o f antibodies as out of an antiserum to proteins. In comparison to this, stroma-free chloroplasts bind 4 times more antibodies to proteins than to lipids. From this it fol­ lows that the major part o f the lipids is located in the m em brane surface which is directed towards the inside or is located inside the mem brane. As the chemical analysis has shown these results are not caused by an altered chemical composition of the m em brane fragments. Despite the fact that m em brane proteins bind considerably less protein antibodies than stroma-free chloroplasts, the antibody binding in m em brane fragment might be considerably increased for certain proteins such as a polypeptide with an apparent molecular weight 24000 and cytochro­ me f. Antibodies to the m ajor components o f the lipid mixture, such as to monogalactosyl diglyce-ride, trigalactosyl diglyceride, sulfoquinovosyl diglyceride and phosphatidyl glycerol are 3 to 4 times more bound by m em brane fragments than by stroma-free chloroplasts. From these results it is concluded that the thylakoid m em brane surface directed towards the inside is preponderently composed of lipids whereas the surface directed towards the outside consists only by 10 to 15% of lipids. 
  Reference    Z. Naturforsch. 34c, 1199—1204 (1979); received July 6 1979 
  Published    1979 
  Keywords    Chloroplasts, Thylakoid M em brane Surface, Proteins, Lipids, Antibodies 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1199.pdf 
 Identifier    ZNC-1979-34c-1199 
 Volume    34 
9Author    Ursula Lehmann-Kirk, KlausP. Bader, G. Eorg, H. Schmid, Alfons RadunzRequires cookie*
 Title    Inhibition of Photosynthetic Electron Transport in Tobacco Chloroplasts and Thylakoids of the Blue Green Alga Oscillatoria chalybea by an Antiserum to Synthetic Zeaxanthin  
 Abstract    An antiserum to synthetic Z eaxanthin inhibits photosynthetic electron transport on the oxygen-evolving side of photosystem II in tobacco chloroplasts and thylakoids o f the filamentous blue-green alga Oscillatoria chalybea. The inhibition site lies for both species between the site o f electron donation of water or tetramethyl benzidine and that o f diphenyl carbazide or manganese II ions. Typical photosystem I reactions are not impaired by the antiserum. The effect of the antiserum concerning the inhibition site is practically identical to that o f the earlier described antiserum to violaxanthin. However, the degree o f inhibition seems to be generally somewhat lower with the antiserum to Zeaxanthin, than with that to violaxanthin which hints at a lesser accessibility of ze-axanthin, in the tylakoid membrane in comparison to violaxanthin. In the course of these investigations new evidence was obtained that the oxygen-evolving side of the electron transport scheme is differently organized in Oscillatoria chalybea when compared to tobacco chloroplasts. Thus, the silicomolybdate reduction with water as the electron donor is sen­ sitive to DCMU in these algae. 
  Reference    Z. Naturforsch. 34c, 1218—1221 (1979); received August 2 1979 
  Published    1979 
  Keywords    Antibodies, Oxygen-Evolving Side, Xanthophylls, Chloroplasts, Blue-Green Algae 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-1218.pdf 
 Identifier    ZNC-1979-34c-1218 
 Volume    34 
10Author    Joseph Veser, H. Elm, Ut ThomasRequires cookie*
 Title    Immunological Studies of Catechol Methyltransferase from the Yeast Candida tropicalis  
 Abstract    Immunization o f rabbits with purified catechol methyltransferase from Candida tropicalis yielded a potent antiserum. Ouchterlony double diffusion analysis showed a single precipitin line. There was no cross reactivity with the catechol methyltransferase from rat and bovine liver. Specific antigen-antibody interaction was demonstrated by a potent inhibitory effect of the antibody on the yeast enzyme. Immunological titration and quantitative precipitin reaction of the enzyme showed that the maximum amount of precipitable complex occurred at the equivalence point where enzyme activity was completely inhibited. 
  Reference    Z. Naturforsch. 35c, 712—7 (1980); received April 24/May 27 1980 
  Published    1980 
  Keywords    Catechol Methyltransferase, Antibodies, Yeast Fungus, Candida tropicalis CBS 94 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0712.pdf 
 Identifier    ZNC-1980-35c-0712 
 Volume    35 
11Author    Z. NaturforschRequires cookie*
 Title    of Saccharomyces cere visiae  
 Abstract    The mating pherom one o f baker's yeast, the a-factor, is a dodeca-/tridecapeptide, which is not antigenic by itself. It was coupled to succinylated thyroglobulin by the car-bodiimide procedure to facilitate selective coupling of the a-factor mainly by its N-terminal region. Antibodies against this conjugate were raised in rabbits. After selective precipitation of the rabbit antiserum with succinylated carrier prior to the radial double diffusion test (Ouchter-lony) specific antibodies against the coupled a-factor could be detected. 
  Reference    Z. Naturforsch. 38c, 1069—1071 (1983); received April 21/Septem ber 5/1983 
  Published    1983 
  Keywords    a-Factor, Antibodies, Pheromone, Saccharomyces cerevisiae 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-1069_n.pdf 
 Identifier    ZNC-1983-38c-1069_n 
 Volume    38 
12Author    RichardJ. Berzborn, Werner FinkeRequires cookie*
 Title    Localization and Orientation of Subunit Delta of Spinach Chloroplast ATP-Synthase within the CF0CF! Complex 1. Distinction of Shielded and Exposed Surfaces of Delta on the Thylakoid Membrane  
 Abstract    A new polyclonal antiserum against spinach CF, subunit delta was produced in rabbits. It decorates only one band at 21 kDa in Western immunoblots of thylakoid proteins and does not react in E LISA with 6-free four subunit C F ,(—6); therefore it is regarded monospecific. The polypeptide used as immunogen had been purified by HPLC. Earlier antisera against CF, 6 cross-react with CF, subunit ß. The new antiserum 306 contains different antibodies; some can be absorbed with thylakoids, i.e. by 6 within the assembled CF0CF, complex on the membrane, others still react in ELISA with isolated CF,. The former antibodies agglutinate thylakoids and inhibit PMS cyclic photophos­ phorylation. Therefore we conclude that part of the surface of CF! subunit 6 is exposed within the quaternary structure of the ATP-synthase complex of photosynthetically active thylakoids, but part of the surface of 6 is shielded. Trypsination of isolated 6 occurs at several sites, but this protease does not attack 6 in situ, nor does aminopeptidase. Staphylococcus aureus protease V8 digests CF, 6 after isolation at residues Asp53, G1u61, G1u95 and G lu 106, but has no access to these residues of 6 in situ. Thus CF, subunit 6 seems to be shielded within the CF0CF, complex to a large degree. Direct agglutination of thylakoids by anti 6 serum 306 was weak and could be improved tenfold by a Coombs serum (goat anti rabbit gammaglobulin), whereas an anti ß serum agglutinated directly. From this we conclude that 6 is not accessible at the top of the enzyme; the exposed part is extending below the large subunits a and ß and oriented towards the membrane. 
  Reference    Z. Naturforsch. 44c, 153 (1989); received June 24/October 7 1988 
  Published    1989 
  Keywords    Accessibility, Antibodies, Coupling Factor, Proteolysis, Photophosphorylation 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0153.pdf 
 Identifier    ZNC-1989-44c-0153 
 Volume    44 
13Author    Walter Oettmeier, Klaus Masson, Ralf Kloos, Ellen ReilRequires cookie*
 Title    On the Orientation of Photosystem II Inhibitors in the QB-Binding Niche: Acridones, Xanthones and Quinones  
 Abstract    The orientation o f acridones, xanthones, 1,4-benzo-and naphthoquinones within the ph o­ tosystem II Q b herbicide-binding niche was studied by means o f mild trypsination and by esti­ mation o f p /50-values in Chlamydomonas reinhardtii D 1 mutants (Val219 > lie, A la25, > Val, Phe255 > Tyr, Ser264 > Ala, A sn266 > Thr, and Leu275 > Phe). A s judged from the R/S-values (ratios o f -^50 -values resistant versus susceptible type) close to 1 in all mutants, the acridones and xanthones do not have strong interactions with the parent amino acids. Contrary, the qui-nones exhibit extreme low R/S-values down to 0.003 (for 2,5-dibrom o-3-m ethyl-6-isopropyl-1,4-benzoquinone; D BM IB) in the Ser264 mutant. This extreme negative cross resistance or supersensitivity indicates that the quinones do not droxyl group. 
  Reference    Z. Naturforsch. 48c, 146—151 (1993); received December 3 1992 
  Published    1993 
  Keywords    Chlamydomonas reinhardtii Mutants, D 1 Protein, Antibody, Trypsination 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0146.pdf 
 Identifier    ZNC-1993-48c-0146 
 Volume    48 
14Author    R. Egina, H. Aase, M. Onika, U. N. Th, U. Tu Rier, A. Lfons, R. Adunz, G. Eorg, H. SchmRequires cookie*
 Title    Determination of Glycolipids, Sulfolipid and Phospholipids in the Thylakoid Membrane  
 Abstract    D eterm ination of binding o f antibodies to lipids onto the surface o f the thylakoid mem­ brane, before and after the removal of the CF,-complex with sodium bromide, showed that in the immediate vicinity of CF, sulfolipid and monogalactolipid occur in higher concentration and are therefore arranged in domains. The m olar ratio of the CF,-complex to glycolipids was determined in Nicotiana tabacum chloroplasts o f different structure. Thus, in the chlorophyll-deficient tobacco m utants N. tabacum Su/su and Su/su var. Aurea, the m olar ratio o f C F ,/ m onogalactolipid is the same and found to be 1:570. The structure o f the lamellar system in these m utants is characterized by a higher ratio o f strom a lamellae to grana stacks when com ­ pared to the green wild type. In the wild type the ratio CF,/m onogalactolipid is 30 per cent larger (1 :740). In contrast to this the m olar ratio CF,/sulfolipid and CF,/digalactolipid is the same in the wild type and the Su/su mutant, whereas these ratios are twice as high in the yellow m utant Nicotiana tabacum Su/su var. Aurea. The binding of glycolipids and phospholipids onto the subunits o f CF, from Spinacia olera-cea was determined in the Western blot procedure by using monospecific antisera. These ex­ periments lead to the result that the two large subunits (a and ß) are m arked by antisera to monogalactosyldiglyceride, digalactosyldiglyceride and sulfoquinovosyldiglyceride. The anti­ sera to phospholipids react differently: whereas the antiserum to phosphatidylinositol only reacts with the a-subunit, the antiserum to phosphatidylcholine and that to phosphatidylgly-cerol react just as the antisera to glycolipids with both large subunits. It is observed that the antiserum to monogalactolipid occasionally m arks the y-subunit. This might mean that the glycolipids and the respective phospholipids are tightly bound onto the reacting a-and ß-subunits of the CF,-complex. Incubation of the subunit CF, with lipase from Rhizopus arrhi-zus and with phospholipase C from Chlostridium perfringens after their transfer to the nitrocel­ lulose membrane abolishes the positive reaction of the peptides with the antisera to glycolipids and phospholipids. 
  Reference    Z. Naturforsch. 48c, 623—631 (1993); received May 17 1993 
  Published    1993 
  Keywords    CF, -Subunits, Glycolipids, Phospholipids, Antibodies, Lipid-Binding 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0623.pdf 
 Identifier    ZNC-1993-48c-0623 
 Volume    48 
15Author    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 
16Author    Irene Alpes, Erwin Stiirzl, Siegfried Scherer, Peter BögerRequires cookie*
 Title    Interaction of Photosynthetic and Respiratory Electron Transport in Blue-Green Algae: Effect of a Cytochrome c-553 Specific Antibody  
 Abstract    An antibody prepared against purified cytochrom e c-553 from Nostoc muscorum inhibits the redox function o f cytochrome c-553 as checked by a diaphorase assay. 20 to 30% inhibition o f NADPH-driven respiratory and light-induced oxygen uptake by Nostoc thylakoids is observed when cytochrome c-553 specific antibodies were applied. H owever, only 30 to 50% o f the total cytochrome c-553 content is released from isolated m em brane m aterial, thus being accessible to antibodies. Supplementing the isolated m embrane m aterial w ith excess Nostoc cytochrom e before adding the antibody abolishes inhibition. The data provide further evidence for soluble cytochrome c-553 being a link between photosynthetic and respiratory electron transport in blue-green algae. 
  Reference    Z. Naturforsch. 39c, 623 (1984); received March 13 1984 
  Published    1984 
  Keywords    Antibody, Cytochrome c-553, Blue G reen-Algae, Cyanobacteria, Interaction Photosynthesis/Respiration 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0623.pdf 
 Identifier    ZNC-1984-39c-0623 
 Volume    39 
17Author    Matthias Kuhn, Andreas Thiel, Peter BögerRequires cookie*
 Title    The 9-kDa Phosphoprotein Involved in Photoinhibition  
 Abstract    Photosystem-II particles exhibit strong photoinhibition. Short-term illumination of photosys-tem-II particles with high-intensity light (5000 piE/m 2 x s) leads to a typical change of the protein pattern on SDS-PAGE. Two proteins are mainly affected, namely the well-described 32-kDa herbicide-binding protein which probably is degraded [1] and, first published here, the 9-kDa phosphoprotein, whose function in the PS-II complex is still unknown. This protein is not de-graded, but seems to be linked to other polypeptides of the PS-II complex. During light treatment new bands of 23, 41, 50 and 54 kDa appear in the protein pattern of SDS-PAGE. A monospecific antiserum was produced against the 9-kDa phosphoprotein to investigate its fate. After light treatment the antibodies reacted with new proteins of higher molecular weights, most pronounced with a 23-kDa and a 41-kDa peptide. 
  Reference    Z. Naturforsch. 43c, 413—417 (1988); received February 15 1988 
  Published    1988 
  Keywords    9-kDa Phosphoprotein, Photosystem-II Particles, Photoinhibition, Protein Phosphorylation, Antibody 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0413.pdf 
 Identifier    ZNC-1988-43c-0413 
 Volume    43 
18Author    AchimE. Gau, Gudrun Wälzlein, Susanne Gärtner, Matthias Kuhlmann, Susanne Specht, ElfriedeK. PistoriusRequires cookie*
 Title    Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    Photosystem II complexes from the cyanobacterium Anacystis nidulans have been investigated by Western blots with antisera raised against four photosystem II peptides from plants and with an antiserum raised against the soluble L-amino acid oxidase protein from/1. nidulans to achieve an iden­ tification of the polypeptides — especially of the L-amino acid oxidase related protein — in isolated photosystem II complexes. Anacystis photosystem II complexes which were solubilized with lauryldimethylamine N-oxide and purified by sucrose cushion and sucrose gradient centrifugation, contained as major Coomassie brilliant blue stained polypeptides a 71 kDa band of unknown identity, a 62 kDa band, which partly contained D-l, a 55 and 49 kDa band which were immuno-reactive with an antiserum to the 47 kDa peptide of tobacco PS II complexes, and three distinct bands in the 30 kDa region. These latter bands could be identified as the extrinsic Mn stabilizing peptide (27—30 kDa), D-l (30—33 kDa) and a 36 kDa peptide (35 — 38 kDa) which crossreacted with the antiserum raised against the soluble L-amino acid oxidase protein of 50 kDa. These results suggest that the 36 kDa peptide present in purified photosystem II complexes from A. nidulans might be a processed form of the soluble 50 kDa L-amino acid oxidase protein. 
  Reference    Z. Naturforsch. 44c, 971—975 (1989); received June 22 1989 
  Published    1989 
  Keywords    Photosystem II, L-Amino Acid Oxidase, Antibody, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0971.pdf 
 Identifier    ZNC-1989-44c-0971 
 Volume    44 
19Author    K. Künzler3, W. Eichenberger3, A. R. AdunzbRequires cookie*
 Title    Intracellular Localization of Two Betaine Lipids by Cell Fractionation and Immunomicroscopy  
 Abstract    The cellular localization of the betaine lipids diacylglyceryl-N,/V,/V-trimethylhomoserine (D G TS) and diacylglycerylhydroxymethyl-/V,./V,/V-trimethyl-ß-alanine (D G T A) was investi­ gated by a) chemical analysis of subcellular fractions and b) immunochemical methods using specific antisera and either fluorescence microscopy or electron microscopy for detection of the label. A homogenate of L ycopodium annotinum (Pteridophyta) was fractionated by differential and density gradient centrifugation. The particulate fractions obtained were ana­ lyzed for chlorophyll, cyt c oxidase, N A D H -cyt c reductase and DGTS. Non-plastidial frac­ tions were enriched in DGTS and only minor amounts o f this lipid could be attributed to chloroplasts. Anti-DGTS and anti-DGTA sera were produced by immunization of rabbits. The monospecificity of the antisera was examined with cells of C hlam ydom onas reinhardtii (Chlorophyceae) containing DGTS, Pavlova lutheri (H aptophyceae) containing DGTA and Ochromonas danica (Chrysophyceae) containing both DGTS and DGTA. Euglena gracilis which is free of betaine lipids, was used as a control. For the test, a FITC-coupled goat anti-rabbit antibody was used and detected by fluorescence microscopy. Thin sections of Ochromonas and Pavlova were incubated first with the anti-lipid sera and subsequently with a gold-coupled anti-rabbit serum and then examined in the electron microscope. With O chro­ monas, anti-DGTS as well as anti-DGTA sera gave an accumulation of gold label in the cytoplasmic space but not in the chloroplasts. Similar results were obtained with Pavlova using anti-DGTA serum. These results describe for the first time the cytochemical localiza­ tion of DGTS and DGTA strongly suggesting both these lipids to be associated mainly with non-plastidial structures. 
  Reference    Z. Naturforsch. 52c, 487—4 (1997); received March 28/May 12 1997 
  Published    1997 
  Keywords    Antibodies, D G TA, DGTS, Immunoelectron Microscopy, Immunofluorescence, Membrane Fractions 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0487.pdf 
 Identifier    ZNC-1997-52c-0487 
 Volume    52 
20Author    Alfons Radunz, Renate MeierRequires cookie*
 Title    Binding o f Antibodies onto the Thylakoid Membrane VII. Localization o f Coupling Factor o f Photophosphorylation in the Lamellar System o f Chloroplasts from Antirrhinum majus  
 Abstract    The maximal binding o f antibodies against the subunits o f the coupling factor o f photo­ phosphorylation onto the ultrasonic sediment and to stroma-freed chloroplasts o f Antirrhinum majus was determined. Different surfaces o f the thylakoid membrane are accessible to antibodies in both chloroplast preparations. Stroma-freed chloroplasts bind antibodies only at the outer sur­ face, which is directed towards the stroma in intact chloroplasts. In the ultrasonic sediment, which is the product of ultrasonication and centrifugation, as was demonstrated by electronmicroscopy, the major part o f the surface directed towards the inside o f the thylakoids is accessible. Both chloroplasts preparations are able to bind different amounts o f antibodies to the five sub­ units of the coupling factor. While antigenic determinants o f all five subunits are present on the surface directed to the outside, the «^-components seems to be lacking on the surface directed 
  Reference    Z. Naturforsch. 37c, 236 (1982); received December 3 1981 
  Published    1982 
  Keywords    Chloroplasts, Thylakoid Membrane, Subunits o f the Coupling Factor, Antibodies, Maximal Binding o f Antibodies 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0236.pdf 
 Identifier    ZNC-1982-37c-0236 
 Volume    37