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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    Magdalena Karamać, Ryszard AmarowiczRequires cookie*
 Title    Inhibition of Pancreatic Lipase by Phenolic Acids -Examination in vitro  
 Abstract    The influence of addition 2, 4, 6, 8, and 10 [j .m of ben­ zoic and cinnamic acids and selected phenolic acids (sali­ cylic, /^-hydroxybenzoic, gentisic, protocatechuic, vanil­ lic, syringic, o-coumaric, p-coumaric, caffeic, ferulic, sinapic) on the activity of pancreatic lipase was exam ­ ined in vitro. The strongest inhibition activities were ob­ served with caffeic, ferulic and benzoic acid, while si­ napic and gentisic acids produced the lowest inhibition. benzoic, /^-hydroxybenzoic, gentisic, vanillic, syrin­ gic, cinnamic, o-coumaric, p-coumaric, caffeic, fer­ ulic, sinapic (all from Sigma). Chemical structures of the compounds m entioned above are described in Fig. 1. o Acids: Benzoic Salicylic p-Hydroxybenzoic Gentisic Protocatechuic Vanillic Syringic R: 4-H R: 2-OH R: 4-OH R: 2,5-di-OH R: 3,4-di-OH R: 3-OCH3, 4-OH R: 3,5-di-OCH3, 4-OH 
  Reference    Z. Naturforsch. 51c, 903—905 (1996); received May 28/September 4 1996 
  Published    1996 
  Keywords    Phenolic Acids, Pancreatic Lipase, Inhibition 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0903_n.pdf 
 Identifier    ZNC-1996-51c-0903_n 
 Volume    51 
3Author    Reinhard Jeck, Christoph WoenckhausRequires cookie*
 Title      
 Abstract    The coenzyme anologues [3-(2-acetylpyridinio) -propyl]-adenosine pyrophosphate and [3-(2-bromo-acetylpyridinio) -propyl] -adenosine pyrophoshate were synthesized and used for inhibition studies. While the first compound reacts as competitive inhi­ bitor against NAD+ , the latter is able to form co­ valently bound derivatives of several NAD+ -depen-dent dehydrogenases, giving informations about amino acid side chains participating in the binding of the functional coenzyme part. [3-(2-acetylpyridinio) -propyl] -adenosine pyro­ phosphate exhibits strong hypochromicity between adenine and 2-acetylpyridine ring. Cleavage of the pyrophosphate bridge increases the absorption at 261 nm up to 22% and indicates, that the stacked configuration of the molecule is preferred in aqueous solution. In enzymatic assays with YADH and GAPDH [3-(2-acetylpyridinio) -propyl] -adenosine pyrophos­ phate acts as a competitive inhibitor against NAD+ . The inhibition constants are: Xi = 1.7'10-2 M (YADH) and 4.3, 10" 4m (GAPDH) and show, that the coenzyme analogue has little affinity to the co­ enzyme binding sites. Difference spectra of the coenzyme-enzyme mixtures and the isolated com­ ponents do not show any spectral changes due to the formation of the binary complex in the case of YADH and only small effects with GAPDH. From this results it can be concluded, that the incorpora­ tion of the 2-acetylpyridinio-propyl residue into the enzymes is sterically hindered. This is also indicated by the fact, that YADH shows smaller inhibition constants with adenosine monophosphate and adeno­ sine diphosphate 1. We obtained [3-(2-bromoacetylpyridinio) -pro­ pyl]-adenosine pyrophosphate by bromination of 
  Reference    (Z. Naturforsch. 29c, 180 [1974]; received) 
  Published    1974 
  Keywords    ) N AD+ -analogues, Dehydrogenases, Inhibition, Affinity Labelling 
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 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0180_n.pdf 
 Identifier    ZNC-1974-29c-0180_n 
 Volume    29 
4Author    Dettmar Von WachtendonkRequires cookie*
 Title    in the Haemolymph of the Mussel M ytilus edulis  
 Abstract    A Cholinesterase deriving from the hemolymph of the mussel M ytilus edulis was partially purified by use of gel-permeation and ion-exchange chromatography; the speci-fity to different substrates or inhibitors indicates clearly the occurrence of a "true" acetylcholinesterase. 
  Reference    (Z. Naturforsch. 31c, 333 [1976]; received October 20 1975/February 9 1976) 
  Published    1976 
  Keywords    M ytilu s edulis, Hemolymph, Acetylcholinesterase, Specificity, Inhibition 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0333_n.pdf 
 Identifier    ZNC-1976-31c-0333_n 
 Volume    31 
5Author    S. Reimer, K. Link, A. TrebstRequires cookie*
 Title    Comparison of the Inhibition of Photosynthetic Reactions in Chloroplasts by Dibromothymoquinone, Bromonitrothymol and Ioxynil  
 Abstract    The inhibition of photosynthetic electron flow in broken chloroplasts by dibromothymoquinone and dibromothymohydroquinone (DBMIBH2) is reversed by dithiothreitol (DTT) as well as by serum albumin. The reversal of DBMIBH2 inhibition by DTT shows a time lag, that of DBMIB only, when chloroplasts and DBMIB had been preilluminated. This is to show that chloroplasts reduce DBMIB and that probably DBMIBH2 is the actual inhibitor species. Bromonitrothymol, ioxynil and related inhibitory phenolic compounds have a different relation­ ship of inhibitory potency to chemical structure than DCMU and the analogous triazinone herbicide metribuzin but nevertheless inhibit photosynthetic electron flow at the same functional site. This is supported by the finding that labelled metribuzin is displaced from the thylakoid membrane by bromonitrothymol and ioxynil indicating identical binding sites. On the other hand inhibition by the phenolic inhibitors bromonitrothymol and ioxynil but not that of DCMU and metribuzin has a time lag of about 4 min. 
  Reference    Z. Naturforsch. 34c, 419 (1979); received October 31 1978 
  Published    1979 
  Keywords    Photosynthesis, Inhibition, Herbicides, Dibromo-thymoquinone, Bromonitrothymol, Ioxynil 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0419.pdf 
 Identifier    ZNC-1979-34c-0419 
 Volume    34 
6Author    KennethW. Right, J. R. CorbettRequires cookie*
 Title    Biochemistry of Herbicides Affecting Photosynthesis  
 Abstract    This paper reviews the inhibitory effects of herbicides at three locations within photosynthetic electron transport, on photophosphorylation, and on pigm ent synthesis. 
  Reference    Z. Naturforsch. 34c, 966 (1979); received May 24 1979 
  Published    1979 
  Keywords    Herbicides, Photosynthesis, Pigm ent Synthesis, Inhibition 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0966.pdf 
 Identifier    ZNC-1979-34c-0966 
 Volume    34 
7Author    Magdolna Droppa, Sándor Dem, G. Ábor, H. OrváthRequires cookie*
 Title    Two Sites of Inhibition of the Photosynthetic Electron Transport Chain by the Herbicide Trifluralin  
 Abstract    The effect o f trifluralin on the photosynthetic electron transport has been investigated by oxygen evolution and thermoluminescence m easurem ents. The results confirm the earlier observations that trifluralin at low concentrations blocks electron transport between the two photosystems probably at the same site as DBMIB does. A t higher concentrations however, trifluralin inhibits the reaction from H aO -*■ /?BQ also and affects the thermoluminescence of chloroplasts in a manner sim ilar to DCM U. These results suggest that trifluralin has a second inhibitory site therefore the use o f trifluralin as a specific inhibitor o f electron transport has to be questioned. 
  Reference    Z. Naturforsch. 36c, 853—855 (1981); received June 25 1981 
  Published    1981 
  Keywords    Herbicide, Inhibition, Photosynthetic Electron Transport, Trifluralin, Thermoluminescence 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0853.pdf 
 Identifier    ZNC-1981-36c-0853 
 Volume    36 
8Author    E. Dith, E. Bert, W. In, M. Olfgang, K. Uecke, R. Laus, C. Am Steiner, Hristian VogelRequires cookie*
 Title    Inhibition of Ergosterol Biosynthesis by Etaconazole in Ustilago maydis  
 Abstract    The triazole fungicide etaconazole (C G A 6 4 251) interferes with the ergosterol biosynthesis in Ustilago m aydis by inhibiting the C-14 dem ethylation o f the sterol nucleus. During the late log growth phase o f U. m aydis a novel endogenous sterol m etabolite (14x-m ethyl-ergosta-8,24(28)-dien-3/?,6a-diol) was discovered and analyzed, which accumulates under the influence o f the fungicide. The structure o f this m etabolite points to a hydroxylation-dehydration m echanism for the introduction o f the double bond at C-5 during the ergosterol biosynthesis. In troduction 
  Reference    Z. Naturforsch. 38c, 28 (1983); received July 22 1982 
  Published    1983 
  Keywords    Fungal Lipids, Ergosterol, Inhibition, Etaconazole, Fungicide 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0028.pdf 
 Identifier    ZNC-1983-38c-0028 
 Volume    38 
9Author    JanF H Snel, D. Irk, N. Aber, JackJ S Van, R. EnsenRequires cookie*
 Title    Formate as an Inhibitor of Photosynthetic Electron Flow  
 Abstract    The effects o f formate on the Hill reaction in isolated broken pea chloroplasts were in­ vestigated. Addition o f formate to chloroplasts has two distinct effects: I. basal electron flow can be stimulated 3-fold; 2. uncoupled electron flow is inhibited. The stim ulating effect is due to uncoupling by formate and appears instantaneous. M axim al inhibition by form ate is only observed after prolonged illumination. The inhibitory action o f form ate on electron flow can be relieved by bicarbonate *. 
  Reference    Z. Naturforsch. 39c, 386—3 (1984); received D ecem ber 21 1983 
  Published    1984 
  Keywords    Photosynthesis, Hill Reaction, Formate, Bicarbonate, Inhibition 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0386.pdf 
 Identifier    ZNC-1984-39c-0386 
 Volume    39 
10Author    Michaela Dane, Kerstin Steinert, Kordula Esser, Susanne Bickel-Sandkötter, Francisco Rodriguez-ValeraRequires cookie*
 Title    Properties of the Plasma Membrane ATPases of the Halophilic Archaebacteria Haloferax mediterranei and Haloferax volcanii  
 Abstract    Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or M n2+. The ATPases require high con­ centrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of H f. mediterranei and H f. vol­ canii, respectively, show different sensitivities to inhibitors of ATP hydrolysis. ATP hydrolysis of isolated H f. mediterranei ATPase was inhibited by N aN 3, which was reported to be specific for F-ATPases, by nitrate and N-ethylmaleimide (NEM), which are specific inhibitors of V-ATPases. ATP hydrolysis of H aloferax mediterranei membranes was not inhibited by DCCD , but [14C]DCCD was bound to a 14 kDa peptide of the isolated, partially purified en­ zyme. Furthermore, the ATPase was inactivated by preincubation with 7-chloro-4-nitro-benzofurazan (NBD-C1). The ATPase activity of H f. volcanii membranes was inhibited by NEM but not by nitrate and N aN 3. SDS gel electrophoresis of the partially purified enzyme of Haloferax mediterranei showed putative ATPase subunits of 53. and 7.5 kDa. Immunoblots showed cross reactivity between a 53 kDa peptide and anti-$ (chloro­ plast F(), as well as between 53, 50 and 47 kDa peptides and an ATPase antibody of Methano-sarcina barkeri. The results will be discussed in context with the placement of the archaebac-terial ATPases (A-ATPases) between F-and V-ATPases. 
  Reference    Z. Naturforsch. 47c, 835—844 (1992); received June 29/September 10 1992 
  Published    1992 
  Keywords    Archaebacteria, Plasma Membrane, ATPase, Subunits, ATP Hydrolysis, Inhibition 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0835.pdf 
 Identifier    ZNC-1992-47c-0835 
 Volume    47 
11Author    Julia Serkedjieva3, Monika Konaklievab, Stefka Dimitrova-Konaklievac, Veneta Ivanova3, Kamen Stefanovb, Simeon PopovbRequires cookie*
 Title    Antiinfluenza Virus Effect of Extracts from Marine Algae and Invertebrates  
 Abstract    Sixty products, derived from marine organisms, typical of the Bulgarian Black Sea coast, were examined for inhibitory activity on the reproduction of influenza viruses in tissue cul­ tures. The antiviral effect was investigated by the reduction of virus infectivity. Using repre­ sentative strains of influenza virus it was shown that apparently the inhibitory effect was strain-specific. The most effective products were further studied in fertile hen's eggs and in experimental influenza infection in white mice. 
  Reference    Z. Naturforsch. 55c, 87—9 (2000); received July 13/September 21 1999 
  Published    2000 
  Keywords    Marine Algae, Marine Invertebrates, Influenza Virus, Inhibition 
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 TEI-XML for    default:Reihe_C/55/ZNC-2000-55c-0087.pdf 
 Identifier    ZNC-2000-55c-0087 
 Volume    55 
12Author    A. Trebst, H. Wietoska, W. Draber, H. J. KnopsRequires cookie*
 Title    The Inhibition of Photosynthetic Electron Flow in Chloroplasts by the Dinitrophenylether of Bromo-or Iodo-nitrothymol  
 Abstract    The O -dinitrophenyl derivatives of 2 -bromo-and 2-iodo-4-nitrothymol are inhibitors of photo­ synthetic electron flow from w ater to NADP or methylviologen, yielding 50% inhibition at 0.5 /xm. Photoreductions by either photosystem I or photosystem II alone are not inhibited. The inhibition site is bypassed by TM PD. The inhibition pattern identical to the one of dibromothymoquinone. It is reduction of plastoquinone. 
  Reference    Z. Naturforsch. 33c, 919 (1978); received October 13 1978 
  Published    1978 
  Keywords    Photosynthesis, Chloroplasts, Inhibition, O-Dinitrophenyl-bromonitrothymol, O-Dinitrophenyl-iodo-nitrothymol 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0919.pdf 
 Identifier    ZNC-1978-33c-0919 
 Volume    33 
13Author    Tadao Asamia, Masatoshi Babab, Hiroyuki Koikec, Yorinao Inouea, Shigeo YoshidaaRequires cookie*
 Title    Halogenation Enhances the Photosystem II Inhibitory Activity of 4-Hydroxypyridines: Structure-Activity Relationships and Their Mode of Action  
 Abstract    A range o f 4-hydroxypyridines were synthesized and their activity as PET inhibitors were investigated with regard to their structural resemblance to plastoquinone in photosynthetic electron transport (PET). The activity o f these com pounds was markedly enhanced upon m od­ ifying their structures: introduction o f halogens into both the 3-and 5-positions o f the pyridine ring and additional substitution at the a-position o f the side chain at 6-position were effective am ong others in enhancing the activity. Insertion o f a phenyl ring into the side chain at 6-position o f the pyridine ring also increased the activity. Substituents on the phenyl ring greatly affected the activity: when substituted with an appropriate functional group, the com ­ pounds became 10-to 100-fold more active. The m ode o f action o f both halogenated and non-halogenated 4-hydroxypyridines were investigated by means o f thermoluminescence measure­ ments and cross resistance examination against atrazine-resistant thylakoids having mutation in D 1 protein. It was inferred that upon halogenation, 4-hydroxypyridines changed their m ode o f action from plastoquinone-pool inhibitors to phenol-type inhibitors. 
  Reference    Z. Naturforsch. 48c, 152 (1993); received October 30 1992 
  Published    1993 
  Keywords    4-Pyridone, 4-Hydroxypyridine, Photosynthetic Electron Transport, Inhibition, Halogenation 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0152.pdf 
 Identifier    ZNC-1993-48c-0152 
 Volume    48 
14Author    Susanne Bickel-Sandkötter, Martina UferRequires cookie*
 Title    Properties of a Dissimilatory Nitrate Reductase from the Halophilic Archaeon Haloferax volcanii  
 Abstract    Grown under anaerobic conditions in presence of nitrate, Haloferax volcanii shows nitrate reduction and accumulation of nitrite in the culture medium. We found a membrane-asso-ciated nitrate reductase, which could easily be solubilized by gently stirring of isolated mem­ branes. Surprisingly, this nitrate reductase requires no NaCl for its activity. A medium pH of 7.5 and high temperatures up to 80 °C are necessary for optimum activity. Kinetic studies showed that the apparent K M was 0.36 mmol/1 for nitrate and 80 ^mol/1 for dithionite-reduced methyl viologen. The respiratory chain inhibitor cyanide effects nitrate reduction noncompe-titively with respect to nitrate with a K \ of 0.3 mmol/1. Azide was a strong inhibitor: The concentration required for half maximal inhibition was 60 |amol/l, whereas thiocyanate and chlorate were much weaker inhibitors. The isolated enzyme was partially purified by frac­ tionated precipitation using polyethylene glycol. SDS gel electrophoresis resulted in three putative subunits of the nitrate reductase of molecular masses of about 100, 61, and 31 kDa. 
  Reference    Z. Naturforsch. 50c, 365—372 (1995); received February 6/February 27 1995 
  Published    1995 
  Keywords    Archaeon, Haloferax volcanii, Dissimilatory Nitrate Reductase, Nitrate Reduction, Inhibition 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0365.pdf 
 Identifier    ZNC-1995-50c-0365 
 Volume    50 
15Author    Agnieszka Bzowska3, Lucyna Magnowska3, Zygmunt KazimierczukbRequires cookie*
 Title    Synthesis of 6-Aryloxy-and 6-Arylalkoxy-2-chloropurines and Their Interactions with Purine Nucleoside Phosphorylase from Escherichia coli  
 Abstract    The phase transfer method was applied to perform the nucleophilic substitution of 2,6-dichloropurines by modified arylalkyl alcohol or phenols. Since under these conditions only the 6-halogen is exchanged, this method gives 2-chloro-6-aryloxy-and 2-chloro-6-arylalkoxy-purines. 2-Chloro-6-benzylthiopurine was synthesized by alkylation of 2-chloro-6-thiopurine with benzyl bromide. The stereoisom ers of 2-chloro-6-(l-phenyl-l-ethoxy)purine were ob­ tained from R-and 5-enantiomers of sec.-phenylethylalcohol and 2,6-dichloropurine. A ll derivatives were tested for inhibition with purified hexameric E. coli purine nucleoside phosphorylase (PNP). For analogues showing IC50 < 10 ^.m, the type o f inhibition and inhibi­ tion constants were determined. In all cases the experimental data were best described by the mixed-type inhibition model and the uncompetitive inhibition constant, Kiu, was found to be several-fold lower than the competitive inhibition constant, Kic. This effect seems to be due to the 6-aryloxy-or 6-arylalkoxy substituent, because a natural PNP substrate adenine, as well as 2-chloroadenine, show mixed type inhibition with almost the same inhibition con­ stants Kiu and K1C . The most potent inhibition was observed for 6-benzylthio-2-chloro-, 6-benzyloxy-2-chloro-, 2-chloro-6-(2-phenyl-l-ethoxy), 2-chloro-6-(3-phenyl-l-propoxy)-and 2-chloro-6-ethoxypur-ines (Kiu = 0.4, 0.6, 1.4, 1.4 and 2.2 [im, respectively). The i?-stereoisomer o f 2-chloro-6-(l-pheny-l-ethoxy)purine has Kiu = 2.0 ^im, whereas inhibition o f its S counterpart is rather weak (IC50> 12 jim). More rigid (e.g. phenoxy-), non-planar (cyclohexyloxy-), or more bulky (2,4,6-trimethylphenoxy-) substituents at position 6 of the purine base gave less potent inhibi­ tors (IC50 = 26, 56 and >100 [im, respectively). The derivatives are selective inhibitors of hexameric "high-molecular mass" PNPs because no inhibitory activity vs. trimeric Cellulomo-nas sp. PNP was detected. By establishing the ligand-dependent stabilization pattern of the E. coli PNP it was shown that the new derivatives, similarly as the natural purine bases, are able to form a dead-end ternary complex with the enzyme and orthophosphate. It was also shown that the derivatives are substrates in the reverse synthetic direction catalyzed by E. coli PNP 
  Reference    Z. Naturforsch. 54c, 1055—1067 (1999); received May 31/August 2 1999 
  Published    1999 
  Keywords    2-Chloropurines, Purine Nucleoside Phosphorylase, Inhibition, Escherichia coli, Phase Transfer Reactions 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-1055.pdf 
 Identifier    ZNC-1999-54c-1055 
 Volume    54 
16Author    Lothar Bornmann, Benno HessRequires cookie*
 Title    Interaction of Cibacron Dyes with Dehydrogenases and Kinases  
 Abstract    Cibacronblue The inhibition of the activity of various kinases and dehydrogenases by Cibacronblue 3 G-A and its structural analogues relies on the interaction of the anthrachinone moiety as well as of the neighbouring phenyl group of the dye with the proteins. Binding is intensified by hydrophobic sub­ stituents at the latter ring system. 
  Reference    (Z. Naturforsch. 32c, 756—759 [1977]; received June 27 1977) 
  Published    1977 
  Keywords    3 G-A, Inhibition, Interaction, Structural Requirement, Kinases and Dehydrogenases 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0756.pdf 
 Identifier    ZNC-1977-32c-0756 
 Volume    32 
17Author    KntonK. HatziosRequires cookie*
 Title    Use o f Isolated L ea f Cells o f A butilon theophrasti to Localize the Action o f Two Aminotriazinone Herbicidal Derivatives  
 Abstract    The effects o f the aminotriazinone herbicides metribuzin [4-amino-6-/er/-butyl-3-(methylthio)-l,2,4,-triazin-5(4H)one] and metamitron [4-amino-3-methyl-6-phenyl-l,2,4-triazin-5(4H)-one] on the metabolism o f enzymatically isolated leaf cells o f Abutilon theophrasti Medic, were examined. Photosynthesis, protein, ribonucleic acid (R N A), and lipid synthesis were assayed by the in­ corporation o f radioactive substrates such as N aH 14C 0 3, [14C]leucine, [14C]uracil, and [14C]acetate, respectively, into the isolated cells. Photosynthesis was the most sensitive process inhibited by both herbicides, but metribuzin was a more potent inhibitor than metamitron. Protein synthesis was not affected by any herbicide. R N A synthesis was inhibited significantly by both herbicides and may be involved in their ultimate herbicidal action. Lipid synthesis was inhibited signifi­ cantly only by the high concentrations o f metribuzin, and it was not affected by any concentration o f metamitron at any incubation time. Inhibition o f lipid synthesis may be involved in the action o f metribuzin as a herbicide. 
  Reference    Z. Naturforsch. 37c, 276—281 (1982); received October 8 December 71981 
  Published    1982 
  Keywords    Abutilon theophrasti, Metabolism o f Isolated Leaf Cells, Metribuzin, Metamitron, Herbicidal Ac­ tion, Inhibition 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0276.pdf 
 Identifier    ZNC-1982-37c-0276 
 Volume    37