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1Author    H. K. KleudgenRequires cookie*
 Title    Die Wirkung von Simazin auf die Bildung der plastidären Prenyllipide in Keimlingen von Hordeum vulgare L. Effect of Simazine on Formation of Chloroplasts Prenyllipids in Seedlings of H ordeum vulgare L  
 Abstract    Barley seedlings were grown for 7, 10 or 13 days under continuous white light (Fluora lamps) on a nutrient solution containing simazine (2-chloro-4,6-bis-(ethylamino)-s-triazine, 10, 100 j u m) . Accumulation of chlorophylls and in part of carotenoids was increasingly enhanced depending on age and concentrations applied. The ratio chlorophyll a/b decreased on this line in 10 and 13 day old plants, the ratio xanthophylls//?-carotene and the ratio chlorophyll a/prenylquinones (plasto-quinone-90x. + red. , a-tocopherol, a-tocoquinone) increased. The way how these prenyllipid ratios are changed in 10 and 13 day old plants is characteristic of a shade type adaptation, as it was shown earlier for other herbicides inhibiting photosystem II. In 7 day old plants the ratio chlorophyll a/prenylquinones decreased. Photosynthetic activity (Hill-reaction) was enhanced in the simazine plants. The ratio chlorophyll a/b was higher, the ratio xanthophylls//?-carotene was lower than in the older seedlings. Similar changes of prenyllipid ratios like in 7 day seedlings and a higher Hill activity were also found in plants grown under blue light (sun type adaptation) as compared to red light (shade type adaptation). This points to similar metabolic changes in the chloroplasts which could be related to a common site of regulation, perhaps the endogenuous cytokinins. The Hill activity, increasing with age in the 10 and 13 day plants, indicates that the mode of action of simazine may be a multiple process resulting to a parallel formation of shade type and sun type characteristics. 
  Reference    Z. Naturforsch. 34c, 110 (1979); eingegangen am 13. November 1978 
  Published    1979 
  Keywords    Herbicide, Simazine, Prenyllipids, Chloroplasts, Regulation 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0110.pdf 
 Identifier    ZNC-1979-34c-0110 
 Volume    34 
2Author    Kassem AlefRequires cookie*
 Title    in Rhodopseudomonas capsulata AD 2  
 Abstract    Nitrate assimilation by Rhodopseudomonas capsulata A D 2 was com pletely inhibited by ammonium only in young well illuminated cultures. At higher densities (A660 about 0.5) the addition o f ammonium had no inhibitory effect, but the nitrate was only reduced to the level o f nitrite, which appeared in the medium. Under both conditions the cellular level o f nitrate reductase activity remained unaffected. In marked contrast to other R. capsulata strains both ammonium sensitive and insensitive cells could reduce nitrate in the light and in the darkness. In the light up to 90% of the reduced nitrate was assim ilated, but in the dark the reduced nitrate was stoichiometrically excreted as nitrite. This behaviour was only shown by R. capsulata A D 2 and BK5, while in other strains the nitrate assim ilation was always com pletely inhibited by ammonium. The role o f photosynthesis and respiration by the regulation o f nitrate reduction is discussed. 
  Reference    Z. Naturforsch. 39c, 85—8 (1984); received Novem ber 10 1983 
  Published    1984 
  Keywords    Nitrate Reduction, Regulation, Rhodopseudomonas capsulata 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0085.pdf 
 Identifier    ZNC-1984-39c-0085 
 Volume    39 
3Author    Peter Westhoff, Kurt Zimmermann, Frank Boege, Klaus ZetscheRequires cookie*
 Title    Regulation of the Synthesis of Ribulose-l,5-bisphosphate Carboxylase and Its Subunits in the Flagellate Chlorogonium elongatum. II. Coordinated Synthesis of the Large and Small Subunits  
 Abstract    Transfer of heterotrophically grown cells of the unicellular green alga Chlorogonium elongatum to autotrophic growth conditions causes a 10 -1 5 fold increase in the amount o f the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase. This increase was found to be due to de novo synthesis. The relative proportions o f large and small subunits o f the enzyme do not change. Their ratio is close to 3.4, the proportions in weight o f the two subunits in the holoenzyme. Continous labelling with [35S]sulfate reveals that the ratios of incorporation into large and small subunits are essentially the same in autotrophic and heterotrophic cells. Pulse-chase experiments show that the subunits are degraded synchronously. The coordinated subunit synthesis cannot be uncoupled using inhibitors o f protein and RNA synthesis or high temperature of cultivation of the alga. The results suggests a very tightly coordinated synthesis o f the large and small subunits of ribulosebisphosphate carboxylase. 
  Reference    Z. Naturforsch. 36c, 942 (1981); received July 18 1981 
  Published    1981 
  Keywords    Ribulose-1, 5-bisphosphate Carboxylase, Synthesis, Subunits, Regulation, Phytoflagellate Chlorogonium elongatum 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0942.pdf 
 Identifier    ZNC-1981-36c-0942 
 Volume    36 
4Author    Divya Mishra, Ahlert SchmidtRequires cookie*
 Title    Regulation and Partly Purification of the ATP-Sulfurylase from the Cyanobacterium Synechococcus 6301  
 Abstract    ATP-sulfurylase from the cyanobacterium Synechococcus 6301 was regulated in vivo during growth in batch culture. The activity was highest at the third day after inoculation, declining afterwards to a level found in resting cells. During growth with air supplemented with 2% CO, this activity increased 3-fold compared to controls grown with normal air as C 0 2 source. Addition o f either nitrite or urea enhanced ATP-sulfurylase activity about 2-fold, whereas cys­ teine and especially methionine decreased ATP-sulfurylase activity to 5% o f controls without treatment. The ATP-sulfurylase was purified by conventional techniques using D EAE-cellulose chro­ matography and further separation on blue sepharose achieving a 250-fold increase in the spe­ cific activity. An apparent o f 5 for APS and o f 40 |iM for pyrophosphate was deter­ mined with the purified enzyme fraction. 
  Reference    Z. Naturforsch. 47c, 95 (1992); received September 26 1991 
  Published    1992 
  Keywords    ATP-Sulfurylase, Cyanobacterium, Synechococcus, Sulfate A ctivation, Regulation 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0095.pdf 
 Identifier    ZNC-1992-47c-0095 
 Volume    47 
5Author    W. N. Oé, H. U. SeitzRequires cookie*
 Title    Studies on the Regulatory Role of fra/is-Cinnamic Acid on the Activity of the Phenylalanine Ammonia-Lyase (PAL) in Suspension Cultures of Daucus carota L  
 Abstract    In vivo and in vitro experiments were performed in order to study the regulatory role of trans-cinnamic acid and its hydroxylated derivatives (p-coumaric acid, caffeic acid) on the deamina­ tion of phenylalanine catalyzed by PAL (EC 7>arts-cinnamic acid inhibits growth and reduces the content of soluble proteins of anthocyanin-containing carrot cells grown in suspen­ sion. There is strong evidence from the polysomal patterns and from the effect of ?ra«5-cinnamic acid on protein synthesis in vitro that protein synthesis is inhibited. The kinetic data of PAL clearly demonstrate that /ra«s-cinnamic acid inhibits the enzyme by a noncompetitive mecha­ nism. On the contrary, L-a-aminooxy-/?-phenylpropionic acid (l-AOPP), a competitive inhibitor of PAL, does not affect protein metabolism. 
  Reference    Z. Naturforsch. 38c, 408 (1983); received January 24 1983 
  Published    1983 
  Keywords    Phenylalanine Ammonia-Lyase, Protein Metabolism, Regulation, /ra/js-Cinnamic Acid, Daucus carota, Suspension Culture 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0408.pdf 
 Identifier    ZNC-1983-38c-0408 
 Volume    38