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1988 (2)
1Author    EgbertJ. Boekema, Günter Schmidt, Peter Gräber, JanA. BerdenRequires cookie*
 Title    Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy  
 Abstract    The structure of the ATP-synthase, F 0 F,, from spinach chloroplasts and beef heart mitochon-dria has been investigated by electron microscopy with negatively stained specimens. The deter-gent-solubilized ATP-synthase forms string-like structures in which the F 0 parts are aggregated. In most cases, the F, parts are arranged at alternating sides along the string. The F 0 part has an approximate cylindrical shape with heights of 8.3 and 8.9 nm and diameters of 6.2 and 6.4 nm for the chloroplast and mitochondrial enzyme, respectively. The F, parts are disk-like structures with a diameter of about 11.5 nm and a height of about 8.5 nm. The F, parts are attached to the strings, composed of F n parts, in most cases, with their smallest dimension parallel to the strings. The stalk connecting F 0 and F, has a length of 3.7 nm and 4.3 nm and a diameter of 2.7 nm and 4.3 nm for the chloroplast and mitochondrial enzyme, respectively. 
  Reference    Z. Naturforsch. 43c, 219—225 (1988); received December 1 1987 
  Published    1988 
  Keywords    ATP-Synthase, Enzyme Structure, Electron Microscopy 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0219.pdf 
 Identifier    ZNC-1988-43c-0219 
 Volume    43 
2Author    Matthias Höpfner, Georg Reifferscheid, Aloysius WildRequires cookie*
 Title    Molecular Composition of Glutamine Synthetase of Sinapis alba L  
 Abstract    Chloroplastic glutamine synthetase of Sinapis alba, purified to homogeneity by a simple three step procedure, revealed a molecular weight of about 395 kDa. The native enzyme is composed of eight subunits of identical molecular weight (about 50 kDa (each), although isoelectrofocusing yielded six distinct bands in the pH 5.6 region of the gel. Labelling of the enzyme with the glutamate analogue herbicide [ 14 C]phosphinothricin and with [y-32 P]ATP indicated that glutamine synthetase has eight reactive centers per molecule. The native enzyme dissociated into two enzymatically active subaggregates of about 195 kDa after Mg 2+ deprivation. 
  Reference    Z. Naturforsch. 43c, 194—198 (1988); received November 26 1987 
  Published    1988 
  Keywords    Active Centers, Enzyme Purification, Enzyme Structure, Glufosinate, Glutamine Synthetase, Phosphinothricin 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0194.pdf 
 Identifier    ZNC-1988-43c-0194 
 Volume    43