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1989 (1)
1988 (1)
1Author    Christine Ziegler, Aloysius WildRequires cookie*
 Title    The Effect of Bialaphos on Ammonium-Assimilation and Photosynthesis II. Effect on Photosynthesis and Photorespiration  
 Abstract    The application of bialaphos (phosphinothricyl-alanyl-alanine) effects a quick photosynthesis inhibition under atmospheric conditions (400 ppm C 0 2, 21% 0 2). However, under conditions (1000 ppm C 0 2, 2% 0 2) under which photorespiration cannot occur there is no photosynthesis inhibition. In the previous investigation it could be shown that bialaphos splits in plants into phosphinothricin and alanine. The inhibition of glutamine synthetase through freed phosphino­ thricin results in an NH4+-accumulation and a decrease in glutamine. With the addition of glutamine, photosynthesis inhibition by bialaphos can be reduced. An NH4+-accumulation takes place under atmospheric conditions as well as under non-photorespiratory conditions; though in the latter case, in less amounts. After adding glutamine and other amino acids the NH4+-accumu-lation increases especially. This indicates that NH4+-accumulation cannot be the primary cause for photosynthesis inhibition by bialaphos. The investigations indicate that for the effectiveness of either bialaphos or phosphinothricin, a process in connexion with photorespiration plays a consid­ erable role. The glyoxylate transamination in photorespiration could be inhibited, which results probably on a glyoxylate accumulation. Corresponding investigations showed inhibition of photo­ synthesis as well as a direct inhibition of RubP-carboxylase with glyoxylate. 
  Reference    Z. Naturforsch. 44c, 103 (1989); received September 23 1988 
  Published    1989 
  Keywords    Ammonium-Accumulation Bialaphos, Phosphinothricin, Photorespiration, Photosynthesis 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0103.pdf 
 Identifier    ZNC-1989-44c-0103 
 Volume    44 
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