Go toArchive
Browse byFacets
Bookbag ( 0 )
'Glutamate Dehydrogenase' in keywords
Results  4 Items
Sorted by   
Section
Publication Year
1984 (1)
1982 (1)
1980 (2)
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 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0406.pdf 
 Identifier    ZNC-1980-35c-0406 
 Volume    35 
2Author    Peter Müller, DietrichW. ErnerRequires cookie*
 Title    Rhizobium japonicum  
 Abstract    Alanine dehydrogenase (E.C. 1.4.1.1.) from nitrogenase repressed free living cells o f Rhizobium japonicum 61-A-101 was purified 370 fold to a specific activity o f 30.4 (imol pyruvate • min-1 • mg protein-1. The same enzyme from effective bacteroids from nodules o f Glycine max var. Mandarin, infected with the same strain was purified 150 fold to a specific activity o f 35 units. The enzyme from both preparations was identical in the molecular weight o f about 168 kD with four identical subunits of 42 kD. The alanine dehydrogenase is, therefore, different from the same enzyme from Bacillus subtilis (molecular weight 228 kD) and from Anabaena cylindrica (molec­ ular weight 270 kD). The K m data for the enzyme from Rhizobium japonicum are: 4.7 mmol/1 for NH+, 0.68 mmol/1 for pyruvate and 44 nmol/1 for NADH. Specific activity o f the enzyme in total cell extracts from eight other strains of Rhizobium japonicum (3 effective strains, 5 ineffective strains) was only 20 to 30% o f the activity with strain 61-A -101. N o correlation between alanine dehydrogenase activity and nitrogenase activity in these other eight strains was observed. The function of alanine dehydrogenase in Rhizobium japonicum in ammonium assimilation and cell wall differentiation is discussed. 
  Reference    Z. Naturforsch. 37c, 927 (1982); received May 19 1982 
  Published    1982 
  Keywords    Rhizobium, Bacteroid Differentiation, Alanine Dehydrogenase, Glutamate Dehydrogenase, Ammonium Assimilation 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0927.pdf 
 Identifier    ZNC-1982-37c-0927 
 Volume    37 
3Author    Heinz-W Alter, Scheid, Adelheid Ehmke, Thomas HartmRequires cookie*
 Title    Plant NAD-Dependent Glutamate Dehydrogenase. Purification, Molecular Properties and Metal Ion Activation of the Enzymes from Lemna minor and Pisum sativum  
 Abstract    Glutamate dehydrogenase (L-glutamate: N A D + oxidoreductase (deaminating) EC 1.4.1.2) has been purified to homogeneity from Lemna minor and seeds o f Pisum sativum. As established by polyacrylamide gel electrophoresis the Pisum-enzyme constitutes a multiple pattern o f seven char­ ge isoenzymes whereas the Lemna enzyme shows one single protein band. Molecular weights of 230 000 were calculated for both enzymes by sedimentation equilibrium measurements (Pisum-enzyme]I and comparative gel filtration (Lemna-enzyme). Sodium dodecyl sulfate gel electropho­ resis and electron microscopic observations revealed that both enzymes are composed of four identical subunits (molecular weight 58 500) arranged in a tetraedric structure. The amino acid compositions of both enzymes are similar to those of various hexameric glutamate dehydrogen­ ases. The N-terminal amino acid of the Pisum-enzyme is alanine. Both enzymes require Ca2+ for maximal catalytic activity. For the Lemna-enzyme the K0.s values for Ca2+ are 22 /j.m (NADH-de-pendent reaction) and 4 piM (N A D +-dependent reaction), respectively. Ca2+ which to some extent can be replaced by Zn2+ does not affect the enzyme aggregation but seems to govern a reversible equilibrium between catalytically active and inactive enzyme forms. 
  Reference    Z. Naturforsch. 35c, 213—221 (1980); received November 21 1979 
  Published    1980 
  Keywords    Lemna minor, Pisum sativum, Glutamate Dehydrogenase, Purification, Molecular Properties, Me­ tal Ion Activation 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0213.pdf 
 Identifier    ZNC-1980-35c-0213 
 Volume    35 
4Author    Z. NaturforschRequires cookie*
 Title    Glutamate Dehydrogenase of Pisum sativum: Heat-Dependent Interconversion of the M ultiple Forms  
 Abstract    Purified NAD-dependent glutamate dehydrogenase (EC 1.4.1.2) from pea seeds shows a pattern o f seven catalytically active molecular forms. The individual forms display different heat stabilities. During incubation at 70 to 75 °C in the presence o f protective agents (N A D H , Ca2+, DTE) the more heat labile forms are converted into the m ost stable form. This result presents direct evidence that the m ultiple forms o f pea glutam ate dehydrogenase represent conform a­ tional variants o f a single protein species. 
  Reference    Z. Naturforsch. 39c, 257 (1984); received N ovem ber 22 1983 
  Published    1984 
  Keywords    Pisum sativum, Glutamate Dehydrogenase, M ultiple Forms, H eat-D ependent Interconversion, Conformational Variants 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0257.pdf 
 Identifier    ZNC-1984-39c-0257 
 Volume    39