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2001 (1)
1Author    DessislavaN. Ikolova, G. Eo Rg Iev A3, Stanka Stoevab, W. Olfgang, V. Oelterb, NicolayG. EnovRequires cookie*
 Title    Viviparus ater Hemocyanin: Investigation of the Dioxygen-Binding Site and Stability of the Oxy-and Apo-Forms  
 Abstract    The active site of Viviparus ater (mollusc) hemocyanin was investigated using the fact that the binding of dioxygen to the binuclear copper-containing sites of hemocyanins is connected with the appearance of specific dichroic bands which are very sensitive to changes in the structrure and polarity of the environment. O xy-V iviparus ater hemocyanin exhibits near UV and visible circular dichroism spectra different from those of other molluscan and arthropo-dan hemocyanins. These differences are due probably to variations in the geometry or charge distribution in the dioxygen binding sites of the com pared proteins. The thermostability of Viviparus ater hemocyanin and the significance of the copper-dioxy-gen system for the stability were also investigated. "M elting" tem peratures, Tm, of 77 °C for the oxy-hemocyanin and 57 °C for the apo-protein were calculated from the denaturation curves which demonstrates the considerable role of the binuclear active site for the therm o­ stability. Viviparus ater hemocyanin is more therm ostable than other hemocyanins for which data are published. 
  Reference    Z. Naturforsch. 56c, 843—847 (2001); received A pril 9/May 18 2001 
  Published    2001 
  Keywords    Dioxygen Transport, Hemocyanin, Mollusc 
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 TEI-XML for    default:Reihe_C/56/ZNC-2001-56c-0843.pdf 
 Identifier    ZNC-2001-56c-0843 
 Volume    56