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1980 (1)
1Author    M.Arianne Nagel, ThomasH. Artm AnnRequires cookie*
 Title    Glutamate Dehydrogenase from Medicago sativa L., Purification and Comparative Kinetic Studies of the Organ-Specific Multiple Forms  
 Abstract    NAD-specific glutamate dehydrogenase [L-glutamate: N A D + oxidoreductase (deaminating) EC 1.4.1.2] from Medicago sativa constitutes organ-specific patterns o f isoenzymes. The isoenzyme-pattems o f seeds (GDH-I) and roots (GDH-II) were purified 1520-fold and 92-fold, respectively. All isoenzymes o f both patterns remain stable throughout the purification procedures. Isoenzyme a7, the only isoenzyme common to both patterns was isolated from the GDH-I pattern. The three enzyme preparations were found to be identical in pH optima, substrate specificity and general ki­ netic properties. A comparative kinetic analysis revealed no pronounced differences between the various kinetic constants evaluated for the three enzyme preparations. Furthermore an identical order of substrate binding and product release could be established. Both initial rate measure­ ments and product inhibition studies are consistent with an ordered ternary-binary kinetic mecha­ nism. The results suggest that tissue-specific enzyme multiplicity of plant glutamate dehydrogen­ ase is not related to differences in general or kinetic properties. 
  Reference    Z. Naturforsch. 35c, 406 (1980); received January 71980 
  Published    1980 
  Keywords    Medicago sativa, Glutamate Dehydrogenase, Multiple Enzyme Forms, Purification, Kinetic Pro­ perties 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0406.pdf 
 Identifier    ZNC-1980-35c-0406 
 Volume    35