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'5 bisphosphate Carboxylase Oxygenase' in keywords Facet   section ZfN Section C  [X]
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1988 (1)
1983 (1)
1Author    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 
2Author    P. M. Abuja, I. PilzRequires cookie*
 Title    Investigation of Ribulose-1,5-bisphosphate Carboxylase-Oxygenase from Tobacco by Small Angle X-Ray Scattering: A Structural Model for the Enzyme in Solution  
 Abstract    The quaternary structure of ribulose-l,5-bisphosphate carboxylase/oxygenase from tobacco (Nicotiana tabacum) was investigated in solution by means of small angle X-ray scattering. The most important molecular parameters as the radius of gyration (Rg) and the maximum diameter (Dmax) were determined. Both the active and the inactive form of the enzyme were measured at 5 °C and at 20 °C. A more distinct difference in size could be detected between the inactive forms at these two temperatures (Rg = 4.80 nm (5 °C) and 4.68 nm (20 °C)) than between the active forms (Rg = 4.73 nm and 4.69 nm). The maximum diameters were determined to be 13.1 nm for the inactive form at 5 °C and 12.8 nm for the other forms. A model is proposed consisting of eight large and eight small subunits arranged in the way that seems to be typical for this enzyme in higher plants. 
  Reference    Z. Naturforsch. 43c, 373—376 (1988); received December 21 1987/February 15 1988 
  Published    1988 
  Keywords    Small-Angle X-Ray Scattering, Solution Structure, Ribulose-l, 5-bisphosphate Carboxylase/ Oxygenase, Conformational Change, Temperature Effect 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0373.pdf 
 Identifier    ZNC-1988-43c-0373 
 Volume    43