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1983 (1)
1981 (1)
1Author    Peter Westhoff, Kurt Zimmermann, Frank Boege, Klaus ZetscheRequires cookie*
 Title    Regulation of the Synthesis of Ribulose-l,5-bisphosphate Carboxylase and Its Subunits in the Flagellate Chlorogonium elongatum. II. Coordinated Synthesis of the Large and Small Subunits  
 Abstract    Transfer of heterotrophically grown cells of the unicellular green alga Chlorogonium elongatum to autotrophic growth conditions causes a 10 -1 5 fold increase in the amount o f the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase. This increase was found to be due to de novo synthesis. The relative proportions o f large and small subunits o f the enzyme do not change. Their ratio is close to 3.4, the proportions in weight o f the two subunits in the holoenzyme. Continous labelling with [35S]sulfate reveals that the ratios of incorporation into large and small subunits are essentially the same in autotrophic and heterotrophic cells. Pulse-chase experiments show that the subunits are degraded synchronously. The coordinated subunit synthesis cannot be uncoupled using inhibitors o f protein and RNA synthesis or high temperature of cultivation of the alga. The results suggests a very tightly coordinated synthesis o f the large and small subunits of ribulosebisphosphate carboxylase. 
  Reference    Z. Naturforsch. 36c, 942 (1981); received July 18 1981 
  Published    1981 
  Keywords    Ribulose-1, 5-bisphosphate Carboxylase, Synthesis, Subunits, Regulation, Phytoflagellate Chlorogonium elongatum 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0942.pdf 
 Identifier    ZNC-1981-36c-0942 
 Volume    36 
2Author    P. Braun, J. Bode, A. WildRequires cookie*
 Title    Ribulose-1,5-bisphosphate Carboxylase-Oxygenase: New Aspects Respective the pH-Dependance of the Carboxylation Reaction  
 Abstract    The investigation was directed towards the effects o f reaction conditions, substrates and pH on the carboxylation reaction of ribulose-1 ,5-bisphosphate carboxylase-oxygenase in the crude enzyme extracts from several plants. O ptim al substrate concentrations (H C O j and RubP) were determined. The highest carboxylase activity was attained with Tris/H Cl buffer. The pH activity profile was quite sharp with an optim um at pH 7.8. Purified and crystallized carboxylase yielded a broad optimum curve under the same reaction conditions. 
  Reference    Z. Naturforsch. 38c, 243—246 (1983); received D ecem ber 6 1982 
  Published    1983 
  Keywords    Ribulose-1, 5-bisphosphate Carboxylase-Oxygenase, C rude Enzyme Extracts, Reaction Conditions, pH Activity Profile 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0243.pdf 
 Identifier    ZNC-1983-38c-0243 
 Volume    38