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'Vanadate' in keywords
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1Author    G. Blasse, G. J. DirksenRequires cookie*
 Title    Luminescence of CS3V2O4F5  
 Abstract    The compound CS3V2O4F5 with statistically distributed [V204F5] 3 ~ complexes shows a weak, red emission at low temperatures. This emission is discussed in relation to similar luminescent compounds. 
  Reference    Z. Naturforsch. 38b, 788—789 (1983); received March 9 1983 
  Published    1983 
  Keywords    Luminescence, Vanadate, Niobate, Tungstate 
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 TEI-XML for    default:Reihe_B/38/ZNB-1983-38b-0788_n.pdf 
 Identifier    ZNB-1983-38b-0788_n 
 Volume    38 
2Author    LudwigJ M Becker, Hans-Ulrich MeischRequires cookie*
 Title    Effect of Vanadate and Iron Stress on the Pigment Composition of Chlorella fusca  
 Abstract    The pigment composition o f Chlorella fusca has been investigated in the absence and in presence of vanadate and during iron stress. 1. Fe-deficiency generally decreases algal pigment content without change of the ratio chloro­ phyll a/b. 2. A twofold vanadate induced increase o f the chlorophylls is accompanied by a similar enhancement o f several xanthophylls, while lutein remains unaffected. 3. Vanadate stimulates the formation o f ^-carotene up to 5 fold, the effect being less obvious during iron stress. 
  Reference    Z. Naturforsch. 36c, 207 (1981); received November 171980 
  Published    1981 
  Keywords    Carotenoids, Chlorella fusca, Chlorophylls, Iron Stress, Vanadate 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0207.pdf 
 Identifier    ZNC-1981-36c-0207 
 Volume    36 
3Author    W. Ilhelm, H. Asselbach, PankajM. Edda, A. Ndrea, M. Igala, BrunoA. GostiniRequires cookie*
 Title    A Conformational Transition of the Sarcoplasmic Reticulum Calcium Transport ATPase Induced by Vanadate  
 Abstract    Vanadate binding to sarcoplasmic reticulum vesicles results in the loss o f the externally located high affinity calcium binding sites o f the calcium transport ATPase. Conversely the occupation by calcium o f the internally located low affinity sites in the vanadate enzym e com plex leads to the release o f vanadate. Since the total num ber o f calcium binding sites is not dim inished by vanadate binding but slightly increases we conclude that vanadate binding induces a transition o f the enzymes external high to internal low affinity calcium binding sites. The transposition o f external to internal calcium binding sites is accom panied by a definite change in the structure o f the sarcoplasmic reticulum membranes. On vanadate binding the asymmetrically arranged electron dense protein particles become symmetrically distributed. 
  Reference    Z. Naturforsch. 38c, 1015 (1983); received Septem ber 14 1983 
  Published    1983 
  Keywords    SR Calcium Transport ATPase, Vanadate, Conformational Transition 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-1015.pdf 
 Identifier    ZNC-1983-38c-1015 
 Volume    38 
4Author    N. Ald, J. Scales, StefanR H IghsmRequires cookie*
 Title     
 Abstract    lec tr o n M ic r o sc o p ic E vid en ce fo r th e T ran sm em b ran e D isp la ce m e n t o f C alcium A T P a se Incubation o f the Ca2+-ATPase in vanadate solutions leads to the formation o f two-dim ensional arrays in the sarcoplasmic reticulum membrane. Electron micrographic freeze fracture replicas show depressions on the inner leaflet for the first time. This indicates that the ATPase has moved perpendicular to the plane o f the m embrane. Our results also suggest that aggregation o f the Ca2+-ATPase into the two-dim ensional arrays occurs before they move into the membrane. These phenom ena were observed as soon as 15 minutes after vanadate was added. The effects o f vanadate appear to be com pletely reversible. When SR was incubated in the vanadate solutions and was then diluted into a buffer containing Ca2+ and ATP, the ATPase activity was normal for up to several hours o f incubation and only somewhat reduced after 3 days. 
  Reference    Z. Naturforsch. 39c, 177 (1984); received May 30/Septem ber 29 1983 
  Published    1984 
  Keywords    Sarcoplasmic Reticulum, Ca2+-ATPase, Ion Transport, Vanadate 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0177_n.pdf 
 Identifier    ZNC-1984-39c-0177_n 
 Volume    39 
5Author    Pankaj Medda, Wilhelm HasselbachRequires cookie*
 Title    Dependence on Membrane Lipids of the Effect of Vanadate on Calcium and ATP Binding to Sarcoplasmic Reticulum ATPase  
 Abstract    The affinity of the sarcoplasmic reticulum transport ATPase for calcium and ATP is not affected by lipid depriviation while vanadate binding is completely abolished. Lipid substitution restores vanadate binding as well as the vanadate induced disappearance of the enzyme's high affinity calcium and nucleotide binding sites. Nucleotide binding is simultaneously restored with the displacement of vanadate from the enzyme following the occupation of its low affinity calcium binding sites. 
  Reference    Z. Naturforsch. 39c, 1137—1140 (1984); received August 31 1984 
  Published    1984 
  Keywords    Sarcoplasmic Reticulum ATPase, Vanadate, Calcium, Adenosinetriphosphate 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-1137.pdf 
 Identifier    ZNC-1984-39c-1137 
 Volume    39 
6Author    P. Ankaj, M. Edda, W. Ilhelm, H. AsselbachRequires cookie*
 Title    Formation and Decay of the Vanadate Complex of the Sarcoplasmic Reticulum Calcium Transport Protein  
 Abstract    The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of magnesium ions approx. 8 nmol monovanadate per mg protein, indicating the formation of a complex containing one vanadate residue per enzyme molecule. On ligand-removal or dilution, the saturated enzyme complex displays biphasic decay kinetics, while the unsaturated complex slowly dissociates monophasically. — Ligand competition by raising the concentrations of un­ labeled vanadate results in a progressive decrease of the dissociation rate of the unsaturated enzyme. The complicated dissociation kinetics indicate a sequential mode of interaction between two ligand binding sites. The one to one stoichiometry of the complex suggests that the two sites are located at adjacent ATPase molecules. — It appears unlikely that the decay of the enzyme, vanadate complex is retarded by the formation of a stable quaternary complex between the enzyme, magnesium, mono-and polyvanadate. 
  Reference    Z. Naturforsch. 40c, 876 (1985); received August 23 1985 
  Published    1985 
  Keywords    Sarcoplasmic Reticulum, Calcium Transport ATPase, Vanadate 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0876.pdf 
 Identifier    ZNC-1985-40c-0876 
 Volume    40 
7Author    Kristine Kranzhöfer, Bruno Agostini, Luisa De, M. Artino, Wilhelm HasselbachRequires cookie*
 Title    Micromorphometric Evaluation of Changes in Symmetry of Sarcoplasmic Reticulum Membranes Induced by Vanadate  
 Abstract    Electron micrographs of light sarcoplasmic vesicles fixed with glutaraldehyde and osmium tetroxide followed by contrasting with uranyl acetate and lead citrate have been evaluated by registering their membrane profiles with a microdensitometer. The asymmetric arrangement o f the two layers of the vesicular membrane could be ascertained by demonstrating a ratio of 1.5 for the thickness o f the outer versus the inner membrane layer which is in general agreement with the proposed protein structure o f the calcium transport enzyme. Treatment of the vesicles with low concentrations of vanadate (0.1 mM) results in a significant lowering of the symmetry ratio by 20% by reducing mainly the thickness of the outer membrane leaflet. Removal of the membrane lipids by treating the vesicles with phospholipase A2 and bovine serum albumin di­ minishes the membrane surface by 50% resulting in a significant increase o f both the mem­ brane thickness and the asymmetry ratio by 30 and 12% respectively. The vanadate induced reduction of membrane asymmetry is accentuated after delipidation indicating that the mem­ brane lipids are not essential for the asymmetric appearance of the native membrane. The sta­ bility of the spherical form o f the vesicles to delipidation implies that the transport molecules are conically shaped allowing strong mutual interactions. At a measured height of the mole­ cule of 80 A in the membrane, the vanadate induced change in symmetry would be brought about by compensatory changes o f less than 3 A of the outer (35 Ä) and the inner (25 Ä) diameter of the cone. 
  Reference    Z. Naturforsch. 47c, 762—772 (1992); received May 19 1992 
  Published    1992 
  Keywords    Sarcoplasmic Reticulum, Membrane Symmetry, Vanadate, Micromorphometry 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0762.pdf 
 Identifier    ZNC-1992-47c-0762 
 Volume    47