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1988 (1)
1Author    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