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1Author    Götz Harnischfeger, Reinhard SchopfRequires cookie*
 Title    A Fluorescence Method for Measuring the Retention of Coupling Factor (CFj) in Reconstitution Experiments of Photophosphorylation  
 Abstract    The recombination of chloroplast coupling factor 1 (CFj) and thylakoid membranes in reconsti­ tution experiments was studied through the fluorescence of paired labels covalently bound to NH,-groups. It was found that maximum recombination is achieved at a ratio of 1.5 —3,ag CF tl/ug chlorophyll. The addition of chloroplast lipids to the medium enhances the incorporation of CFt into the membranes. The rates of ATP formation of the regenerated but labeled system are decreased to 50% of those found in unlabeled control experiments. This is discussed in context with the previous observation, that labeling of CFX at similar concentrations inhibits the ATPase activity of the isolated protein completely. The possible use of double labeling in the study of the physical aspects of the reconstitution of the photophosphorylating system is discussed. 
  Reference    (Z. Naturforsch. 32c, 392 [1977]; received January 26/February 16 1977) 
  Published    1977 
  Keywords    Fluorescence Label, Coupling Factor 1, Reconstitution, Photophosphorylation 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0392.pdf 
 Identifier    ZNC-1977-32c-0392 
 Volume    32 
2Author    Stefan Zabori, Rainer Rudolph, Rainer JaenickeRequires cookie*
 Title    Folding and Association of Triose Phosphate Isomerase from Rabbit Muscle  
 Abstract    The enzymatic activity and quaternary structure o f rabbit muscle triose phosphate isomerase remains unchanged in the concentration range from 2 ng/m l to 2 ng/m l. In this concentration range the enzyme can be reactivated after dissociation and denaturation in 6.5 m guanidine hydrochloride. Removal of the denaturant by dilution and separation o f inactive wrong aggregates (5-20%) lead back to active dimers, indistinguishable from the native enzyme as far as enzymatic and physicochemical properties are concerned. Based on the long term stability o f the enzyme, the reactivation kinetics were analyzed at low concentrations and 0 °C, conditions where the association of inactive monomers to active dim ers is predom inant in the process of reactivation. The concentration dependence of the rate of reactivation and the kinetic profiles could be described by a consecutive first-order folding and second-order association reaction scheme with the rate constants k ^ = 1.9 x 10~2 s-1 and kbi = 3 x 105 m _1 • s~\ This implies that the folded monomers o f triose phosphate isomerase, which are interm ediate states during reconstitution, cannot possess appreciable enzymatic 
  Reference    Z. Naturforsch. 35c, 999—1004 (1980); received A ugust 7 1980 
  Published    1980 
  Keywords    Association, Folding, Reconstitution, Triose Phosphate Isomerase 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0999.pdf 
 Identifier    ZNC-1980-35c-0999 
 Volume    35 
3Author    G. Ünther Bernhardt, Rainer Rudolph, Rainer JaenickeRequires cookie*
 Title    Reassociation of Lactic Dehydrogenase from Pig Heart Studied by Cross-Linking with Glutaraldehyde  
 Abstract    Cross-linking with glutaraldehyde has been successfully applied in order to analyze the kinetics of reassociation of oligomeric enzymes (R. Hermann, R. Rudolph, and R. Jaenicke Nature 277, 243-245 (1979)). In the present study the assembly of lactic dehydrogenase from pig heart is investigated using this approach. In order to eliminate perturbations caused by excessive folding reactions, acid dissociation was performed in the presence of 0.8 M Na2S 0 4 at 0°C . Under optimum conditions complete cross-linking of the tetrameric enzyme was achieved in less than 2 minutes. Cross-linking during reconstitution proves the dimer to be the only intermediate of reasso­ ciation. The dimer -*■ tetramer transition is found to be rate-limiting for both reassociation and reactivation, suggesting the tetramer to be the enzymatically active species. The presence of monomers during reconstitution indicates that tetramer formation is preceded by a fast monomer-dimer equilibrium. The kinetic model describing the experimental data 4M^2D^T is characterized by an equilibrium constant K = 3 ± 1 • 107 liter • m ol-1, and a second-order rate constant k = 1.4 ± 0.2 • 104 liter • mol-1 • s-1. 
  Reference    Z. Naturforsch. 36c, 772—777 (1981); received May 15 1981 
  Published    1981 
  Keywords    Cross-Linking, Glutaraldehyde, Lactic Dehydrogenase, Reassociation, Reconstitution 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0772.pdf 
 Identifier    ZNC-1981-36c-0772 
 Volume    36 
4Author    JesperV. Møller, TalaatS. Mahrous, JensP. Andersen, Marc Le, MaireRequires cookie*
 Title    Functional Significance of Quaternary Organization of the Sarcoplasmic Reticulum Ca2+-ATPase  
 Abstract    There is both structural and functional evidence for protein-protein interaction between Ca2+-ATPase polypeptide chains in the sarcoplasm ic reticulum membrane. Studies on detergent solubilized ATPase indicate that the m onom eric form is capable o f performing a normal cycle o f ATP hydrolysis, but som e o f the m odulatory effects o f the substrates disappear after detergent solubilization. However, the necessity o f protein-protein interactions for the Ca2+ transport function remains unclarified. A new approach is described, em ploying A TPase reconstituted with a large excess o f phospholipid, which m ay help to resolve this question. 
  Reference    Z. Naturforsch. 37c, 517—521 (1982); received February 4 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum Ca2+-ATPase, Protein-Protein Interactions, Reconstitution 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0517.pdf 
 Identifier    ZNC-1982-37c-0517 
 Volume    37 
5Author    G. Ünter Schmidt, PeterG. RäberRequires cookie*
 Title    The Rate of ATP Hydrolysis Catalyzed by Reconstituted CF0F i-Liposomes  
 Abstract    The conditions for optimal rates of ATP hydrolysis catalyzed by the chloroplast ATP-synthase (A T P ase), CFoF,, after isolation and reconstitution into asolectin liposomes have been investi­ gated. The rate of ATP hydrolysis was m easured either after oxidation of CF0F, (by incubation with iodosobenzoate) or after reduction of CFoF, (by incubation with dithiothreitol). In both cases a rate of about 1 -2 A TP (CF0F i-s)" ' was observed under uncoupled conditions. If the pro-teoliposom es are first energized by an acid-base transition and a K"/valinomycin diffusion po ten ­ tial, the uncoupled rate of A TP hydrolysis is about 1 -2 A TP (CFnF, -s) '1 for the oxidized enzyme and about 20 for the reduced species. This rate is about a factor 2 smaller than that observed in chloroolasts under the same conditions. 
  Reference    Z. Naturforsch. 42c, 231 (1987); received O ctober 17 1986 
  Published    1987 
  Keywords    A TP Hydrolysis, ATP Synthase, A TPase, Reconstitution, CF0F, Liposomes 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0231.pdf 
 Identifier    ZNC-1987-42c-0231 
 Volume    42 
6Author    M. Onika, Meyer, Christian WilhelmRequires cookie*
 Title    Reconstitution of Light-Harvesting Complexes from Chlorella fusca (Chlorophyceae) and Mantoniella squamata (Prasinophyceae)  
 Abstract    D edicated to Professor W. Rüdiger (München) on the occasion o f his 60 th anniversary Reconstitution experiments o f light-harvesting complexes were performed with the green alga Chlorella fusca and the chlorophyll c-eontaining prasinophyte M antoniella squamata using a modified method according to Plumley and Schmidt [Proc. N atl. Acad. Sei. U .S.A . 84, 146 -1 5 0 (1987)]. Changing the pigment supply quantitatively or qualitatively in the reconsti­ tution mixture hom ologous and heterologous reconstitutes were obtained. In contrast to higher plants, light-harvesting polypeptides from green algae are able to bind the chlorophylls as well as the xanthophylls in different stoichiometries. H eterologous reconstitutes o f M . squamata polypeptides give further evidence for a rather high flexibility o f pigment recog­ nition and binding. This is the first report o f successful reconstitution o f a chlorophyll c-binding protein. Contrary to chlorophyll c-less light-harvesting com plexes, the reconstitu­ tion o f M . squamata is strongly pH-controlled. In summary, the results give evidence for a high specificity o f porphyrin ring recognition and variability in xanthophyll binding capacity. Therefore, it is suggested that at least in algal light-harvesting proteins chlorophyll organiza­ tion may be determined by other mechanisms than xanthophyll binding. 
  Reference    Z. Naturforsch. 48c, 461 (1993); received December 12 1992/April 1 1993 
  Published    1993 
  Keywords    Algae, Reconstitution, Light-Harvesting Complex, Photosynthesis, Pigment-Protein Inter­ action 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0461.pdf 
 Identifier    ZNC-1993-48c-0461 
 Volume    48