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1993 (1)
1987 (1)
1Author    Thom As Urbig, Rüdiger Schulz, H. Orst SengerRequires cookie*
 Title    Inactivation and Reactivation of the Hydrogenases of the Green Algae Scenedesmus obliquus and Chlamydomonas reinhardtii  
 Abstract    The hydrogenases of the green algae Scenedesmus obliquus and Chlamydomonas reinhardtii were activated under anaerobic conditions. Exposure o f whole cells and cell-free homogenates to air lead to a complete inactivation of the hydrogenases. The inactivation in whole cells of Scenedesmus is faster than the inactivation of the cell-free homogenate. Inactivation o f the hy­ drogenases could be reversed by anaerobic readaptation in whole cells. The inactivation of the hydrogenase in homogenates seems to be irreversible. N either the removal o f oxygen nor the addition of ATP, N AD(P)H, sodium dithionite, dithiothreitol, ferredoxin and thioredoxin to homogenates facilitated the reactivation o f the hydrogenase. The occurrence of a hydrogenase regulating factor is discussed. 
  Reference    Z. Naturforsch. 48c, 41 (1993); received September 30/December 21 1992 
  Published    1993 
  Keywords    Scenedesmus obliquus, Chlamydomonas reinhardtii, Hydrogenase, Reactivation Process, Inactivation 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0041.pdf 
 Identifier    ZNC-1993-48c-0041 
 Volume    48 
2Author    A. Lberto Mazzini, R. Oberto FavillaRequires cookie*
 Title    The Effect of Guanidinium Chloride on the Self-Association of Bovine Liver Glutamate Dehydrogenase: A Gel Filtration Study  
 Abstract    The associative behaviour of bovine liver glutamate dehydrogenase has been studied by gel chrom atography at neutral pH in 1 m guanidinium chloride and 1 m sodium chloride. In guanidinium chloride both the elution volume and the elution profile of the enzyme are independ­ ent of protein concentration, whereas in sodium chloride they are strongly dependent on it. In NaCl the enzyme behaves as expected according to the well established random association m odel, w hereas in guanidinium chloride it appears to have completely lost the self-associative property. F urtherm ore, since the elution volume of the enzyme in guanidinium chloride corre­ sponds to that of an hexamer, trim er formation reported to occur in these conditions is not confirmed !?'7 this technioue 
  Reference    Z. Naturforsch. 42c, 217 (1987); received O ctober 17 1986 
  Published    1987 
  Keywords    G lutam ate D ehydrogenase, Self-Association, Guanidine Chloride, Inactivation, Gel Filtration 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0217.pdf 
 Identifier    ZNC-1987-42c-0217 
 Volume    42