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'Glutathione Reductase' in keywords
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1991 (1)
1984 (1)
1Author    DaivaA. Bironaitė, N. Arim, K. Čėnas, JuozasJ. Kulys, AlexanderG. Medentsev, VasiliyK. Akimenko, P. A. Karplus, E. F. Pai, G. E. Schulz, EurJ. BiochemRequires cookie*
 Title      
 Abstract    Fully substituted quinones including som e naturally occurring oxyquinones acted as inhibitors o f yeast gluta­ thione reductase (EC 1.6.4.2). They were competitive, mixed or uncompetitive inhibitors for N A D P H , possess­ ing K j in the range o f 1 -2 0 0 |iM and uncompetitive in­ hibitors for glutathione. Rhein (4,5-dioxy-9,10-anthra-quinone-2-carbonic acid) and 9,10-phenanthrenequi-none were the most effective inhibitors. It is concluded that certain quinones can bind to the N A D P(H)-binding site and to the heteroaromatics binding site at the inter­ face domain (o f the enzyme. 
  Reference    Z. Naturforsch. 46c, 966—9 (1991); received March 4/M ay 71991. 178 6 9 3 -7 0 3 1989 
  Published    1991 
  Keywords    Glutathione Reductase, Inhibition, Quinones 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0966_n.pdf 
 Identifier    ZNC-1991-46c-0966_n 
 Volume    46 
2Author    AnnaM M Ata, Juan López-BareaRequires cookie*
 Title    Purification by Affinity Chromatography of Glutathione Reductase (EC 1.6.4.2) from Escherichia coli and Characterization of such Enzyme  
 Abstract    The glutathione reductase from Escherichia coli strain S33 was purified to homogeneity by a simple and fast procedure consisting of two affinity chromatography steps. After 40-80% ammonium sulfate fractionation, the enzyme was adsorbed to an N 6-2'.5'-ADP-Sepharose affinity column from which it was specifically eluted by a 0 -10 m M N ADP+ linear gradient. The enzyme was finally purified to homogeneity after a second affinity chromatography step in a C8-ATPR-Sepharose column, from which it was eluted by means of the same N AD P+ gradient. 
  Reference    Z. Naturforsch. 39c, 908—915 (1984); received December 16 1983/April 26 1984 
  Published    1984 
  Keywords    Escherichia coli, Glutathione Reductase, Purification by Affinity Chromatography, Molecular and Kinetic Characterization, Redox Inactivation under Reducing Conditions 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0908.pdf 
 Identifier    ZNC-1984-39c-0908 
 Volume    39