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1981 (1)
1980 (1)
1Author    Estrella Legaz, Carlos VicenteRequires cookie*
 Title    Location of Several Enzymes of L-Arginine Catabolism in Evernia prunastri Thallus  
 Abstract    Agmatine ureo: hydrolase, which produces both putres-cine and urea from agmatine, and urease, which hydrolyzes this urea, are highly restricted to the phycobiont cells in E. prunastri thallus. Arginase and L-arginine decarboxylase, which catabolize L-arginine, have a more extensive dis­ tribution between both symbiotic partners. 
  Reference    Z. Naturforsch. 36c, 692—693 (1981); received March 301981 
  Published    1981 
  Keywords    Arginase, L-Arginine Decarboxylase, Agmatine Ureo: Hy­ drolase, Urease, Evernia prunastri 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0692_n.pdf 
 Identifier    ZNC-1981-36c-0692_n 
 Volume    36 
2Author    P. Grunwald, W. G. Unßer, K. P. Pfaff, R. K. Rause, K. LutzRequires cookie*
 Title    Zur Beeinflussung der Aktivität von adsorptiv auf eloxierten Aluminiumblechen immobilisierter Urease durch die Anodisier-Bedingungen The Influence o f Anodizing Conditions on the Activity o f Urease Immobilized to Anodized Sheet A lum inium  
 Abstract    The activity of urease immobilized by adsorption on anodized sheet aluminium strongly depends on the method chosen for preparation of these carriers. If oxalic acid is applied as electrolyte, only the anodizing temperature significantly influences the activity of the prepara­ tions. In case of the well-known GS process, however, the activity is not only affected by the temperature, but also by other conditions of anodizing, for example the current density and the electrolyte concentration. For both methods the correlation between the topography of the carrier surfaces and the activity of enzyme immobilized to the surface is described. 
  Reference    Z. Naturforsch. 35c, 819—823 (1980); eingegangen am 15. Februar/6. Mai 1980 
  Published    1980 
  Keywords    Immobilized Enzymes, Urease, Anodized Sheet Aluminium, Surface Structure, Scanning Elec­ tron Microscopy 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0819.pdf 
 Identifier    ZNC-1980-35c-0819 
 Volume    35