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'5 bisphosphate Carboxylase' in keywords
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1981 (1)
1980 (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    GünterF. Wildner, PrafullachandraV. Sane, Jürgen HenkelRequires cookie*
 Title    The Activation of Ribulose-l,5-bisphosphate Carboxylase-Oxygenase from Spinach by Oxygen Changes of the Enzyme Conformation during Air-Argon Transitions  
 Abstract    The effect of oxygen on ribulose-l,5-bisphosphate carboxylase-oxygenase from spinach was in­ vestigated. Both activities were deactivated by removal of oxygen and reversibly reactivated by oxygenation of the enzyme solution. The change in enzyme activities was accompanied by confor­ mational changes as studied by the use of intrinsic and extrinsic fluorescent probes. The analysis of cysteine sulfhydryl groups accessible to 5,5'-dithiobis-(2-nitrobenzoic acid) re­ vealed that the number of these groups changed with the oxygen concentration. The kinetic of the exposure of eight cysteine residues was similar to the loss of enzyme activities. The modification of these groups with 5,5'-dithiobis-(2-nitrobenzoic acid) caused almost complete loss of both the activities. The enzyme isolated from a photolithotrophic organism, Chromatium vinosum, was not affected by oxygen removal. During air — argon transitions, neither the enzyme conformation nor the num­ ber of accessible sulfhydryl groups changed. 
  Reference    Z. Naturforsch. 35c, 239—248 (1980); received December 12 1979 
  Published    1980 
  Keywords    Ribulose-l, 5-bisphosphate Carboxylase, Ribulose-l, 5-bisphosphate Oxygenase, Enzyme Confor­ mation, Oxygen Effect, Photosynthesis 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0239.pdf 
 Identifier    ZNC-1980-35c-0239 
 Volume    35