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1984 (230)
1Author    Requires cookie*
 Title    Neuartige Ceramide aus Cystobacter fuscus (Myxobacterales)  
 Abstract    N o v e l C e ra m id e s fro m C y sto b a c te r f u s c u s (M y x o b a c te r a le s) H. Eckau. D. Dill und H. Budzikiew icz Institut für Organische C hem ie der U niversität zu Köln, G re in stra ß e 4. D -5000 K öln 41 Z. Naturforsch. 39c, 1 -9 (1984); received O ctober 31, 1983 Cystobacter, M yxobacterales, C eram ides, C aro ten o id s, M yxobactone From cell m aterial o f Cystobacter fu sc u s strain C b 685 (M yxobacterales) the ceram ides 2 S ,3 Ä -N -(2 'Ä -h y d ro x y -1 5 '-m eth y lp alm ito y l)-1 7 -m eth y lsp h in g a-4 £ ,8 £ -d ien in e (1), 2 S .3 R -N -(2'/?-hydroxypalm itoyl)-17-m ethylsphinga-4£',8£'-dienine (10), 2 S ,3 /?-N -(2 '/? -h y d ro x y -1 5 '-m ethyl)-17-m ethyl-4£-sphingenine (11) and 2S,.3 /? -N -(2 '^ -h y d ro x y -1 5 '-m e th y lp a lm ito y l)-1 7 
  Reference    Z. Naturforsch. 39c, 1 (1984) 
  Published    1984 
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 Identifier    ZNC-1984-39c-0001 
 Volume    39 
2Author    Requires cookie*
 Title    Pistillarin  
 Abstract    , ein charakteristischer Inhaltsstoff der Herkuleskeule (Clavariadelphus pistillaris) und einiger Ramaria-Arten (Basidiomycetes) P istilla rin , a C h a r a c te r is tic M e ta b o lite o f C la v a ria d e lp h u s p is tilla r is 
  Reference    Z. Naturforsch. 39c, 10 (1984) 
  Published    1984 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0010.pdf 
 Identifier    ZNC-1984-39c-0010 
 Volume    39 
3Author    JohnL. Ingham, KennethR M ArkhamRequires cookie*
 Title    New Dextrorotatory Pterocarpan Phytoalexins from Leaflets of Nissolia fruticosa  
 Abstract    Legum inosae. Papilionoideae. Nissolia, Isoflavonoids, (-t-)-Pterocarpans Three isoflavonoid phytoalexins pro d u ced by the fungus o r C u S 0 4-trea te d leaflets o f Nissolia fruticosa have been iden tified as (+)-6 a S ; 1 la 5 -3 .7 -d ih y d ro x y -9 -m eth o x y p tero c arp a n (nissi-carpin). (+)-6 aS ; 1 la S -7-hy d ro x y -3 ,9 -d im eth o x y p tero carp an (fru tic arp in) and (+)-6 a.S; 11 aS-3,7-dihydroxy-2,9-dim ethoxypterocarpan (nissolicarpin). 
  Reference    Z. Naturforsch. 39c, 13—1 (1984); received S eptem ber 26. 1983 
  Published    1984 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0013.pdf 
 Identifier    ZNC-1984-39c-0013 
 Volume    39 
4Author    JeffreyRequires cookie*
 Title    6-Hydroxyflavones and Other Flavonoids of Crocus  
 Abstract    B. H arb o rn e an d C hristine A. W illiam s Phytochem ical U nit, D e p artm en t o f Botany, U niversity o f R eading. Reading. R G 6 2AS. England Z. N aturforsch. 3 9 c, 1 8 -2 3 (1984); received N ovem ber 14. 1983 Iridaceae, Crocus, F lavonoids. K aem pferol G lycosides, C hem otaxonom y. 6 -H ydroxyflavones have been identified for the first tim e in the Iridaceae, in leaves o f three Crocus species. T hree new glycosides have been characterised: 6 -hydroxyluteolin 7-rham nosyl-glucoside, scutellarein 7-glucoside an d scutellarein 7-m ethyl ether 6 -glucoside, as well as two know n glycosides: 6 -hydroxyluteolin 7-glucoside and 6 -hydroxyluteolin 7-m ethyl ether 6 -glucoside. 6 -H ydroxyluteolin and scutellarein glycosides have been found before in Bromeliaceae. Com m elinaceae, C y p eraceae an d O rchidaceae, but this is the first record o f the respective 7-m ethyl ethers in the M onocotyledoneae. A cacetin an d tricin have been identified as aglycones in C. laevigatus a n d C. heuffelianus leaves, respectively and the occurrence o f m angiferin confirm ed in C. aureus leaves. Two o f the m ajor flavonol glycosides present in flowers o f cultivated species w ere identified as kaem pferol 3-sophoroside and kaem pferol 3-rutinoside-7-glucoside. H ow ever none o f the flavonoids identified appears to c ontribute to yellow petal colour in Crocus, w hich is p ro b ab ly entirely carotenoid-based. 
  Reference    Z. Naturforsch. 39c, 18 (1984) 
  Published    1984 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0018.pdf 
 Identifier    ZNC-1984-39c-0018 
 Volume    39 
5Author    Thom As, H. Artm, Ann Klaus, Bax, R. Enate ScholzRequires cookie*
 Title    Aliphatic 1-Amino Acid Decarboxylase from Ferns (Filicopsida)  
 Abstract    azeutische Biologie der T ech nischen U n iv e rsitä t B raunschw eig, M endels-sohnstr. 1, D-3300 Braunschweig. B undesrepublik D eutschland Z. N aturforsch. 39c, 2 4 -3 0 (1984); received S eptem ber 26, 1983 Ferns, Filicopsida, Polypodium vulgare. A lip h atic 1-Amino Acid D ecarboxylase, Occurrence and D istribution A screening o f 27 fern species (F ilicopsida) o u t o f 9 fam ilies revealed th a t 25 species w ere able to decarboxylate 1-leucine to 3 -m ethylbutylam ine (isoam ylam ine). T he enzym e o f P olvpodium vulgäre has partially been p urified and characterisized. All a tte m p ts to solubilize it from acetone preparations failed; however, approx. 50% o f total activity could be extracted from dry m aterial in the presence o f detergents at high concentration. T he soluble enzym e w as p u rifie d 132-fold. 1-Methionine was found the best substrate follow ed by n orvaline, leucine, norleucine, isoleucine, hom ocysteine, valine. It has been confirm ed th a t these su b strates are d e ca rb o x y la ted by a single enzyme. The pH -optim um was at pH 5.0 (p a rticu la te p re p a ra tio n) and pH 4.5 (soluble enzym e). D ecarboxylation is dependent on p y rid o x al-5 '-p h o sp h a te (PL P). A strictly su b stra te d ep en d en t coenzyme dissociation was observed w hich could largely be p re v en ted by additio n o f 2 -oxo-acids, such as glyoxylate or pyruvate. A podecarboxylase p re p are d by p rolonged su b stra te in cu b atio n was found to be extrem ely labile at pH 4.5 but stable at pH 6.5. A co m p ariso n o f the fern enzym e with bacterial valine decarboxylase (EC 4.1.1.14) and leucine decarb o x y lase o f red algae revealed great sim ilarities especially in substrate specificity. It is suggested to unify these activities as "aliphatic 1-am ino acid decarboxylase" . 
  Reference    Z. Naturforsch. 39c, 24 (1984) 
  Published    1984 
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 Identifier    ZNC-1984-39c-0024 
 Volume    39 
6Author    FourcRequires cookie*
 Title    Elaboration of the 6,7,8 Oxygenation Pattern in Simple Coumarins: Biosynthesis of Puberulin in Agathosma puberula  
  Reference    Z. Naturforsch. 39c, 31 (1984) 
  Published    1984 
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 Identifier    ZNC-1984-39c-0031 
 Volume    39 
7Author    L.R G Alagovsky, A. M. Porto, G. Burton, E.G G RosRequires cookie*
 Title    Biosynthesis of the Bufadienolide Ring of Scillirosid in Scilla maritima  
  Reference    Z. Naturforsch. 39c, 38 (1984) 
  Published    1984 
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 Identifier    ZNC-1984-39c-0038 
 Volume    39 
8Author    Requires cookie*
 Title    Ein Adsorbens als Speicher ftir Phytohormone in einer pflanzlichen Suspensionskultur  
 Abstract    An A dsorbent a s P h y to h o rm o n e R eservoir in a P la n t C ell S u sp en sio n C ulture R olf Beiderbeck und Bernd K noop 
  Reference    Z. Naturforsch. 39c, 45 (1984) 
  Published    1984 
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 Identifier    ZNC-1984-39c-0045 
 Volume    39 
9Author    Hartmut Kayser, EmM. RichRequires cookie*
 Title    Hormone Induced Changes in Carotenoid Composition in Ricinus Cell Cultures. I. Identification of Rhodoxanthin  
 Abstract    When cell cultures o f Ricinus communis are grown in light and with kinetin as the sole growth factor red cells are formed. The red pigmentation is due to the accum ulation o f rhodoxanthin which is the major carotenoid in these cultures. The identification o f this retro-type carotenoid is based on electronic and mass spectra, on chemical transformation to zeaxanthin, and on comparison with an authentic sample. Rhodoxanthin is not present in any part o f the intact plant. The major yellow carotenoid in the red cultures is lutein. 
  Reference    Z. Naturforsch. 39c, 50 (1984); received November 10. 1983 
  Published    1984 
  Keywords    Rhodoxanthin Carotenoids, Plant Cell Cultures, Plant Horm ones, Ricinus communis 
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 Identifier    ZNC-1984-39c-0050 
 Volume    39 
10Author    Piotr Lassota, Ryszard Stolarski, David ShugarRequires cookie*
 Title    Conformation about the Glycosidic Bond and Susceptibility to 5 '-Nucleotidase of 8-Substituted Analogues of 5'-G M P  
 Abstract    Guanosine-5'-phosphate, 8-Substituted Analogues, M olecular C onform ation, 5'-N ucleotidase, Ribose-5-phosphate 
  Reference    Z. Naturforsch. 39c, 55 (1984); received August 9 1983 
  Published    1984 
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 Identifier    ZNC-1984-39c-0055 
 Volume    39 
11Author    MichelJacques Polverelli, Ulrich, Robert TeouleRequires cookie*
 Title    Identification of N^Glycolylbiuret in the Gamma Radiolysis of Aerated Aqueous Solution of Cytosine. Influence of the pH  
 Abstract    Cytosine. Gamma-Irradiation. N 1 G lycolylbiuret, pH-Effect N 1 glycolylbiuret has been identified as a radiation product o f cytosine in aerated aqueous solution at pH 4.5. When varying the pH o f the solution before irradiation from acidic values towards neutral ones. G value o f N 1 glycolylbiuret reached a m axim um at pH 4.5. 
  Reference    Z. Naturforsch. 39c, 64 (1984); received March 28/A ugust 8. 1983 
  Published    1984 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0064.pdf 
 Identifier    ZNC-1984-39c-0064 
 Volume    39 
12Author    ToshihisaO. Hshim, Matsumi Ohshim, G.Erhart DrewsRequires cookie*
 Title    Rhodopseudomonas capsulata  
 Abstract    Soluble N A D H Dehydrogenase, Purification, FM N -Sepharose 6 B. A ffinity Chrom atography, Rhodopseudomonas capsulata, Flavins Soluble N A DH dehydrogenase was purified to hom ogeneity from chem otrophically grown cells o f Rhodopseudomonas capsulata by am m onium sulfate fractionation, A H -Sepharose 4B chromatography and FM N -Sepharose 6 B affinity chromatography. The enzym e contains a single polypeptide chain o f an apparent M r o f 37000, suggesting that the subunit structure is different from that o f the membrane-bound enzyme. The purified soluble N A D H dehydrogenase requires flavin compounds, e.g., FM N, FA D and riboflavin, for activity. A ddition o f FM N and FA D . but not riboflavin, to the enzyme solution stabilized the enzyme. The pH optim um for activity was at 7.5. The enzyme was specific for N A D H as an electron donor while N A D P H was inert. Menadione, ferricyanide, cytochrome c and DCIP served as an electron acceptor. The M ichaelis constants for N A DH . DCIP, FM N . and cytochrom e c were 45, 2.9. 7.9 and 15 |iM, respectively. Many properties o f soluble N A D H dehydrogenase were substantially different from those o f the membrane-bound enzyme, suggesting different functions. 
  Reference    Z. Naturforsch. 39c, 68 (1984); received September 26. 1983 
  Published    1984 
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 Identifier    ZNC-1984-39c-0068 
 Volume    39 
13Author    Ken GotoRequires cookie*
 Title    in Lemna  
 Abstract    Biochemical aspects o f circadian rhythms were studied using a long-day duckweed, Lem na gibba G 3 cultured in short day condition (9 h light at 3800 lux follow ed by 15 h darkness), which was transferred in continuous light (LL) at the end (LL 0) o f the last night period. With such a system I have previously reported a rhythm o f affinity for N A D + o f cytoplasm ic N A D -dependent glyceraldehyde 3-phosphate dehydrogenase (C yt-N A D -G P D) 180° out o f phase with that o f affinity for N A D P + o f chloroplastic N A D P -dependent G PD (C h l-N A D P -G P D) and that N A DP+ could increase in vitro the affinity for N A D P + o f C h l-N A D P -G PD . I report here that NA D P+ can decrease in vitro the affinity for N A D + o f C yt-N A D -G P D as well, and furthermore, that the in vivo level o f N A D P + oscillates in phase with the rhythm o f the affinity for N A D P + o f Chl-NADP-GPD. Moreover, I found the existence o f m irror-image circadian rhythms, o f com parable am pli­ tudes, o f in vivo levels o f N A D + + N A D H (total N A D) (with peaks, as the ones o f C yt-N A D -GPD. at LL 0 and 24) and o f N A D P + + N A D P H (total N A D P) (with peaks, as the ones o f Chl-NADP-G PD, at LL 12 and 36). Consequently, a circadian rhythm in the rate o f net in vivo production o f total N A D P (or N A D) m ight be expected 90° in advance o f that in the level o f total NADP (or N A D). Indeed. I found oscillations in the activities o f N A D kinase and o f NA DP phosphatase with peaks occurring, respectively, at LL 6 and at LL 18. Moreover, in vitro treatments with EGTA (a Ca2+-chelator), chlorprom azine and W 7 (both inhibitors o f cal­ modulin) were able to both inhibit N A D kinase from its highest level o f activity to its m inim al one and activate N A D P phosphatase from its lowest level o f activity to its maxim al one. I conclude, therefore, that the in vivo level o f C a2+-calm odulin could oscillate in phase with the rhythm o f N A D kinase activity and induce the mirror-image circadian rhythms o f activities o f NA D kinase and o f NA D P phosphatase. I propose that the control sequence among the several circadian rhythms I studied could start with changes in Ca2+-calm odulin, then proceed through oscillations in N A D kinase and N A D P phosphatase activities, leading to changes in N A D +, N A D P +, and N A D P H levels, which would themselves induce the C hl-N A D P -G PD and C yt-N A D -G P D rhythms. 
  Reference    Z. Naturforsch. 39c, 73 (1984); received June 16/Septem ber 19 1983 
  Published    1984 
  Keywords    Ca2+-Calmodulin, Circadian Rhythms, G lyceraldehyde 3-Phosphate Dehydrogenases (EC 12 
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 Identifier    ZNC-1984-39c-0073 
 Volume    39 
14Author    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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 Identifier    ZNC-1984-39c-0085 
 Volume    39 
15Author    Helmar Almon, Peter BögerRequires cookie*
 Title    Nickel-Dependent Uptake-Hydrogenase Activity in the Blue-Green Alga Anabaena variabilis  
 Abstract    Nickel Requirement, Cyanobacterium . Blue-Green Algae. Hydrogenase. Light-Induced Hydrogen Evolution. Nitrogenase Uptake-hydrogenase activity in the blue-green alga (cyanobacterium) Anabaena variabilis is dependent on the presence o f nickel. Nickel depletion leads to an enhancement o f net light-induced hydrogen evolution, which is catalyzed by nitrogenase. Addition o f nickel chloride to the culture reverses this effect by stim ulating hydrogenase activity. M ethylviologen/dithionite-driven hydrogen formation o f perm eabilized cells is decreased by nickel depletion. 
  Reference    Z. Naturforsch. 39c, 90 (1984); received Decem ber 9 1983 
  Published    1984 
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 Identifier    ZNC-1984-39c-0090 
 Volume    39 
16Author    ElenaA. Kotova, MarinaD. Il 'inaRequires cookie*
 Title    Effect of Electron Transfer Inhibitors and Uncoupling Agents on the Chlorophyll Fluorescence Lifetime during Slow Fluorescence D ecline in Bean Leaves and Intact Chloroplasts  
 Abstract    Fluorescence m easurem ents were performed with bean leaves and intact chloroplasts, which are characterized by a slow fluorescence decline. The fluorescence lifetime (r) ana the fluores­ cence relative quantum yield (q>) o f intact chloroplasts, measured with the phase fluorometer, showed nearly proportional light-induced decrease with a halftime o f ~ 3 0 s, which was removed by 3-(3.4-dichlorophe n y l)-1.1 -dimethylurea (DC M U), by 4.5,6,7-tetrachloro-2'-trifluoromethyl-benzimidazole (TTFB). by carbonyl cyanide /?-trifluoromethoxyphenylhydrazone (FCCP) at a low concentration and by gramicidin D. Simultaneously the slow light-induced increase in absorbance at 518 nm (A A 518), reflecting thylakoid membrane energization, was elim inated. The data on r o f intact chloroplasts are original, the other results agree with literature data. In leaves, the slow light-induced fluorescence decline, with r dropping from ~ 2 to ~ 0.6 ns, was abolished by FCCP at a concentration o f 5 ^m. However, while r was stabilized at a level close to the initial (maximum) one or som ewhat higher, q> became close to the minimum value. Besides, the amplitude o f A A 518 was lowered about three times. These effects seemed to be due to multiple action o f FCCP as a protonophoric uncoupler and an electron transfer inhibitor. In the presence o f another uncoupling agent, TTFB, which, besides, is a diuron-like inhibitor o f the electron transfer in chloroplasts, we observed the light-dependent, but hardly linked to changes in membrane potential, great increase in r o f a leaf from ~ 1.9 to ~ 4 .3 ns, with cp decreasing slightly. Addition o f DC M U together with FCCP to the incubation medium or infiltration o f a leaf with DCM U alone stimulated the rise in r only to ~ 3 ns. The increase in r o f a leaf observed in the presence o f FCCP and DCM U, and especially with TTFB, may be associated with protein conformation changes which (i) alter the lifetime o f nanosecond recombination lum inescence o f the photosystem II a n d /o r (ii) disturb excitation energy transfer from the light-harvesting chlorophyll a /b com plex to other pigment-protein complexes. 
  Reference    Z. Naturforsch. 39c, 93—101 (1984); received October 5 1983 
  Published    1984 
  Keywords    Photosynthesis, C hlorophyll Fluorescence Lifetime, Electron Transfer Inhibitors, Uncouplers, Bean Leaves, Intact Chloroplast 
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 Identifier    ZNC-1984-39c-0093 
 Volume    39 
17Author    Berthold Kiefer, Helmut Sapper, WolfgangL. Ohm AnnRequires cookie*
 Title    The Influence of Amino Acid Ligands and Vitamin C on the Reduction Potential of Fe(III): Polarographie and Electron Spin Resonance Investigations  
 Abstract    The pH dependence o f Fe(III)-am ino acid com plexes has been studied polarographically and by means o f ESR spectroscopy. It could be shown that, at least, two com plexes exist: one with a low m olecular weight, ESR detectable at acid pH. and one with a high molecular w eight at alkaline pH, ESR non detectable. The half wave potential o f Fe (III) is lowered by am ino acid ligands. The redox interaction o f the Fe(III)-amino acid com plexes with vitam in C results in a decrease o f the ascorbyl radical concentration. Ascorbic acid also forms a com plex with Fe(III) as in­ dicated by a polarographic half wave potential near -0.55 V vs. S.C.E. at pH 7. 
  Reference    Z. Naturforsch. 39c, 102—106 (1984); received September 22 1983 
  Published    1984 
  Keywords    Ferrous Ions Ascorbic Acid, Redox-Potential, Polarography, ESR -Spectroscopy 
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 Identifier    ZNC-1984-39c-0102 
 Volume    39 
18Author    Berg, M. Arjo, Brandse Duphar, B. V. BiochemistryRequires cookie*
 Title    G erard van den  
 Abstract    The effects of the algicide PH 40-62 on photosynthetic reactions in spinach chloroplasts were studied. The compound proved to be an uncoupler o f photophosphorylation, whereas inhibition of photosynthetic electron transport occurred at higher concentrations. The site of this inhibition was before photosystem II. The uncoupling effect was partially reversible. In a series o f related compounds the uncoupling activity appeared mainly dependent on the lipophilic properties o f the compounds but electronic effects also played a distinct role. C om paring these uncoupling data with those of some known series of uncouplers it appeared that lipophilicity determ ines the uncoupling activity in an identical way and a regression equation was found describing the uncoupling activities of 60 compounds belonging to four chemically different groups of com ­ pounds. 
  Reference    Z. Naturforsch. 39c, 107—114 (1984); received Septem ber 19 1983 
  Published    1984 
  Keywords    Arylethanediamines, Photophosphorylation, U ncouplers, Structure-Activity Relationships 
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 Identifier    ZNC-1984-39c-0107 
 Volume    39 
19Author    H. Artm, K. L. Ichtenthaler, D. Ieter, M. EierRequires cookie*
 Title    Inhibition by Sethoxydim of Chloroplast Biogenesis, Development and Replication in Barley Seedlings  
 Abstract    Chloroplast Biogenesis, Inhibition of Chloroplast Replication, Sethoxydim. Sun-Type Chloroplast Sethoxydim not only blocks leaf growth and developm ent of barley seedlings but also inhibits chloroplast biogenesis at all stages of development from proplastids to prochloroplasts, young and mature chloroplasts. Not only thylakoid synthesis, thylakoid multiplication and grana for­ mation are affected, but also chloroplast replication. The chloroplasts o f secondary leaves which before the sethoxydim application are in the stage o f young, developing chloroplasts, remain in this differentiation stage when treated with sethoxydim. With their "ultrastructural characteristics (e.g. lower stacking degree, higher proportion o f exposed mem branes, a lower thylakoid frequency etc.) they resemble sun-type chloroplasts. In the shoot meristem sethoxydim-treated plants contain only proplastids, whereas the plastids in the shoot meristem o f control plants are already in the developmental stage between prochloroplasts to young chloroplasts. Mesophyll cells o f sethoxydim-treated plants contain only one third of the chloroplasts found in the controls. 
  Reference    Z. Naturforsch. 39c, 115 (1984); received N ovem ber 17 1983 
  Published    1984 
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 Identifier    ZNC-1984-39c-0115 
 Volume    39 
20Author    R. Obert, B. Mellor, E. Rhard, M. Örschel, D. Ietrich, W. ErnerRequires cookie*
 Title    Legume Root Response to Symbiotic Infection. Enzymes of the Peribacteroid Space  
 Abstract    N ovem ber 2, 1983 Glycine m ax, Mannosidase, Peribacteroid Space. Rhizobium Three of the major soluble partitioned pools in the sym biotic cell, namely the host cell cytoplasm, the cytoplasm of the bacterial symbiont and the space between the two partners (the peribacteroid space) were assayed for selected enzymes. W hilst alanine dehydrogenase was found almost totally in the bacterial cell cytoplasm, other enzymes were more widely spread. Amongst these a-mannosidase, previously described as a vacuolar m arker enzyme in eukaryotes, was found largely in the peribacteroid space. These results are discussed in relation to models o f peribacteroid m em brane biogenesis. 
  Reference    Z. Naturforsch. 39c, 123—125 (1984); received 
  Published    1984 
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 Identifier    ZNC-1984-39c-0123 
 Volume    39 
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