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1981 (1)
1Author    Eckhard Kumpe, H. Ans-G, Erhard Löffler, Friedhelm SchneiderRequires cookie*
 Title    Studies on the Zn2+/C o2+ Exchange with Acylamino Acid Amidohydrolase from Pig Kidney Co2+-Acylamino Acid Amido Hydrolase  
 Abstract    The kinetics of inactivation o f the Zn2+-metalloenzyme acyl-amino acid amido hydrolase by chelating ligands were studied. The rate of inactivation by 1,10-phenanthroline is enhanced by histidine and inhibited in the presence of phenyl-alanine. Removal of the metal ion increases the heat stability and decreases the pH stability of the enzyme. Reactivation o f the inactive metal free enzyme is possible with Zn2+ and Co2+. Titration of the metal free protein with a Co2+/nitrilotriacetate metal buffer revealed a dissociation constant of about 10~7 M for the Co2+ enzyme (Zn2+ enzyme = 10-10m). The Co2+ substituted enzyme is less stable than the Zn2+ < enzyme. Histidine and phenylalanine protect the Co2+ enzyme against inactivation by 1,10-phenanthroline. 
  Reference    Z. Naturforsch. 36c, 951—955 (1981); received June 261981 
  Published    1981 
  Keywords    Chelating Ligands, Co2+ Dissociation Constant, Apo-Enzyme 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0951.pdf 
 Identifier    ZNC-1981-36c-0951 
 Volume    36